Pathogenesis of Brucella

References

• Cotton W. E., Buck J. M. Further researches on Bang's disease. J. Am. Vet. Med. Assoc. 1932; 33: 342
   Google Scholar
• Small P. I. C., Isberg R. R., Falkow S. Comparison of the ability of enteroinvasive Escherichia coli, Salmonella ryphimurium, Yersinea pseudotuberculosis and Yersinea enterocolitica to enter and replicate within HEp-2 cells. Infect. Immun. 1987; 55: 1674
   PubMed Web of Science ®Google Scholar
• Isbert R. R., Voorhis D. L., Falkow S. Identification of invasin: a protein that allows enteric bacteria to penetrate cultured mammalian cells. Cell 1987; 50: 769
   PubMed Web of Science ®Google Scholar
• Falkow S., Small P., Isberg R., Hayes S. F., Corwin D. A molecular strategy for the study of bacterial invasion. Rev. Inf. Dis. 1987; 9((Suppl. 5))S450
   Google Scholar
• Pomales-Lebron A., Stinebring W. R. Intracellular multiplication of Brucella abortus in normal and immune mononuclear phagocytes. Proc. Soc. Exp. Biol. Med. 1957; 94: 78
   PubMed Web of Science ®Google Scholar
• Cheers C. Pathogenesis and cellular immunity in experimental mu-rine brucellosis. Dev. Biol. Stand. 1984; 56: 237
   PubMedGoogle Scholar
• Smith H., Keppie J., Pearce H., Fuller R., Williams A. E. The chemical basis of the virulence of Brucella abortus. I. Isolation of Br. abortus for bovine foetal tissue. Br. J. Exp. Pathol. 1961; 42: 631
   PubMedGoogle Scholar
• Pearce J. H., Williams A. E., Harris-Smith P. W., Fitzgeorge R. B., Smith H. The chemical basis of the virulence of Brucella abortus. II. Erythritol, a constituent of bovine foetal fluids which stimulates the growth of Br. abortus in bovine macrophages. Br. J. Exp. Pathol. 1962; 43: 31
   Google Scholar
• Keppie J., Williams A. E., Witt K., Smith H. The role of erythritol in the tissue localization of the brucellae. Br. J. Exp. Pathol. 1965; 46: 104
   PubMedGoogle Scholar
• Sarram M., Feiz J., Foruzandeh M., Gazanfarpour P. Intrauterine fetal infection with Brucella melitensis as a possible cause of second trimester abortion. Am. J. Obstet. Gynecol. 1974; 119: 657
   PubMed Web of Science ®Google Scholar
• Lamont R. J., Postlethwaite R., MacGowan A. P. Listeria monocytogenes and its role in human infection. J. Infect. Dis. 1988; 17: 7
   Google Scholar
• Lubani M., Sharda D., Helin I. Probable transmission of brucellosis from breast milk to a newborn. Trop. Geogr. Med. 1988; 40: 151
   PubMedGoogle Scholar
• Mackaness M. B. The immunological basis of acquired cellular resistance. J. Exp. Med. 1964; 120: 105
   PubMed Web of Science ®Google Scholar
• Splitter G. A., Everlith K. M. Collaboration of bovine T lymphocytes and macrophages in T-lymphocyte response to Brucella abortus. Infect. Immun. 1986; 51: 776
   PubMed Web of Science ®Google Scholar
• Limet J., Plommet A. M., Dubray G., Plommet M. Immunity conferred upon mice by anti-LPS monoclonal antibodies in murine brucellosis. Ann. Inst. Pasteur Immunol. 1987; 138: 417
   PubMedGoogle Scholar
• Kreutzer D. L., Dreyfus L. A., Robertson D. C. Interaction of polymorphonuclear leukocytes with smooth and rough strains of Brucella abortus. Infect. Immun. 1979; 23: 737
   PubMed Web of Science ®Google Scholar
• Riley I. K., Robertson D. C. Ingestion and intracellular survival of Brucella abortus in human and bovine polymorphonuclear leukocytes. Infect. Immun. 1984; 46: 224
   PubMed Web of Science ®Google Scholar
• Gorham S. L., Enright R. M., Snider T. G., Roberts E. D. Morphologic lesions in Brucella abortus infected ovine fetuses. Vet. Pathol. 1986; 23: 331
   PubMed Web of Science ®Google Scholar
• Meador V. P., Deyoe B. L. Experimentally induced Brucella abortus infection in pregnant goats. Vet. Res. 1986; 47: 2337
   Web of Science ®Google Scholar
• Corner L. A., Alton G. G. Persistence of Brucella abortus strain 19 infection in adult cattle vaccinated with reduced doses. Res. Vet. Sci. 1981; 31: 342
   PubMed Web of Science ®Google Scholar
• Goodpasture E. W., Anderson K. The problem of infection as presented by bacterial invasion of the chorioallantoic membrane for chick embryos. Am. J. Pathol. 1937; 13: 149
   PubMedGoogle Scholar
• Metzger H. J., Stokes F. R. Incubating hen's eggs as a culture medium for B. abortus. J. Am. Vet. Med. Assoc. 1940; 96: 369
   Google Scholar
• Detilleux P. G., Cheville N. F., Deyoe B. L. Pathogenesis of Brucella abortus in chick embryos. Vet. Pathol. 1988; 25: 138
   PubMed Web of Science ®Google Scholar
• Feldman W. H., Olson C. The pathogenicity of Brucella abortus for white mice. J. Infect. Dis. 1935; 5: 212
   Google Scholar
• Dishon T., Olitski L. Lethal Brucella infections in white mice produced with the aid of the mucin technic. Proc. Soc. Exp. Biol. Med. 1949; 71: 698
   PubMed Web of Science ®Google Scholar
• Cheers C., Pagram F. Macrophage activation during experimental murine brucellosis: a basis for chronic infection. Infect. Immun. 1979; 23: 197
   PubMed Web of Science ®Google Scholar
• Birmingham J. R., Jeska E. L. Characterization of macrophage functions in mice infected with Brucella abortus. Infect. Immun. 1981; 32: 1079
   PubMed Web of Science ®Google Scholar
• McCullough N. B. Microbial and host factors in the pathogenesis of brucellosis. Infectious Agents and Host Reactions, S. Mudd. W. B. Saunders, Philadelphia 1970; 342
   Google Scholar
• Holland J. J., Pickett M. J. Intracellular behavior of Brucella variants in chick embryo cells in tissue culture. Proc. Soc. Exp. Biol. Med. 1956; 93: 476
   PubMed Web of Science ®Google Scholar
• Braun W., Pomales-Lebron A., Stinebring W. R. Interactions between mononuclear phagocytes and Brucella abortus strains of different virulence. Proc. Soc. Exp. Biol. Med. 1958; 97: 393
   PubMed Web of Science ®Google Scholar
• Stinebring W. R., Kessel R. Continuous growth of Brucella abortus in mononuclear phagocytes of rats and guinea pigs. Proc. Soc. Exp. Biol. Med. 1959; 101: 412
   PubMed Web of Science ®Google Scholar
• Freeman B. A., Vana L. R. Host-parasite relationships in brucellosis. I. Infection of normal guinea pig macrophages in tissue culture. J. Infect. Dis. 1958; 102: 258
   PubMed Web of Science ®Google Scholar
• Freeman B. A., Kross D. J., Circo R. Host-parasite relationships in brucellosis. II. Destruction of macrophage cultures by Brucella of different virulence. J. Infect. Dis. 1961; 108: 333
   PubMed Web of Science ®Google Scholar
• McGhee J. R., Freeman B. A. Osmotically sensitive Brucella in infected normal and immune macrophages. Infect. Immun. 1970; 1: 146
   PubMedGoogle Scholar
• Buchmeier N., Heffron F., personal communication
   Google Scholar
• Freeman B. A., Pearson G. R., Hines W. D. Host-parasite relationships in brucellosis. III. Behavior of avirulent Brucella in tissue culture monocytes. J. Infect. Dis. 1964; 114: 441
   PubMed Web of Science ®Google Scholar
• Nesthus I., Haneberg B., Glitte J., Solberg C. O. The influence of antimicrobial agents on macrophage-associaied Staphy-lococcus aureus. Acta Pathol. Microbiol. Immunol. Scand. Sect. B 1985; 98: 189
   Google Scholar
• Gay B., Mauss H., Sanchez-Teff S. Identification of fibro-nectins in peritoneal macrophages during the phagocytosis of Brucella, Virchows. Arch. [Ceil Pathol.] 1986; 52: 169
   Web of Science ®Google Scholar
• Young E. J., Borcbert M., Kretzer E. L., Musher D. M. Phagocytosis and killing of Brucella by human polymorphonuclear leukocytes. J. Infect. Dis. 1985; 151: 682
   PubMed Web of Science ®Google Scholar
• Baker I. A., Campbell P. A. Thioglycollate medium decreases resistance to bacterial infection in mice. Infect. Immun. 1980; 27: 455
   PubMed Web of Science ®Google Scholar
• Spitalny G. L. Dissociation of bactericidal activity from other functions of activated macrophages in exudates induced by thioglycolate medium. Infect. Immun. 1981; 34: 274
   PubMed Web of Science ®Google Scholar
• van Dissel J. T., Stikkelbroeck J. J. M., Michel B. C., Leijh P. C. J., van Furth R. Salmonella ryphimurium-specific difference in rate of intracellular killing by resident peritoneal macrophages from Salmonella resistant CBA and Salmonella-suspectible C57BL/10 mice. J. Immunol. 1987; 138: 4428
   PubMedGoogle Scholar
• Smith L., Heffron F., unpublished observation
   Google Scholar
• Anderson T. D., Cheville N. F. Ultrastructural morphometric analysis of Brucella abortus-infected trophoblasts in experimental pla-centitis. Am. J. Pathol. 1986; 124: 226
   PubMed Web of Science ®Google Scholar
• Fields P. I., Swanson R. V., Haidaris C. G., Heffron F. Mutants of Salmonella typhimurium that cannot survive within the macrophage are avirulent. Proc. Natl. Acad. Sci. U.S.A. 1986; 83: 5189
   PubMed Web of Science ®Google Scholar
• Pommier C. G., Inada S., Fries L., Takahashi T., Frank M. M., Brown E. J. Plasma fibronectin enhances phagocytosis of opsonized particles by human peripheral blood monocytes. J. Exp. Med. 1983; 157: 1844
   PubMed Web of Science ®Google Scholar
• Gay B., Mauss H., Sanchez-Teff S. Aspects ultrastructuraux de la phagocytose in vivo et in vitro de Brucella par les macrophages du peritoine de la souris. Ann. Immunol. (Inst. Pasteur) 1981; 132D: 299
   Google Scholar
• Young E. J. Brucella melitensis hepatitis: the absence of granulomas. Ann. Intern. Med. 1979; 91: 414
   PubMed Web of Science ®Google Scholar
• Young E. J., Gomez C. I., Yawn D. H., Mustier D. M. Comparison of Brucella abortus and Brucella melitensis infections of mice and their effect on acquired cellular resistance. Infect. Immun. 1979; 26: 680
   PubMed Web of Science ®Google Scholar
• Spink W. W. The Nature of Brucellosis. University of Minnesota Press, Minneapolis 1956; 112
   Google Scholar
• Hoyer B. H., McCullough N. B. Polynucleotide homologies of Brucella deoxyribonucleic acids. J. Bacleriol. 1968; 95: 444
   PubMed Web of Science ®Google Scholar
• Hoyer B. H., McCullough N. B. Homologies of deoxyribonucleic acids from Brucella ovis canine abortion organisms and other Brucella species. J. Bacterial. 1968; 96: 1783
   PubMed Web of Science ®Google Scholar
• Verger J.-M., Grimont F., Griraont P. A. D., Grayon M. Brucella, a monospecific genus as shown by deoxyribonucleic acid hybridization. Int. J. Syst. Bacleriol. 1985; 35: 292
   Google Scholar
• Allardet-Servent A., Bourg G., Ramuz M., Pages M., Bellis M., Roizes G. DNA polymorphism in strains of the genus Brucella. J. Bacterol. 1988; 170: 4603
   PubMed Web of Science ®Google Scholar
• Ficht T., unpublished observation
   Google Scholar
• Ficht T. A., Bearden S. W., Sowa B. A., Adams L. G. A 36 kDa Brucella abortus cell envelope protein is encoded by repeated sequences closely linked in the genomic DNA. Infect. Immun. 1988; 56: 2036
   PubMed Web of Science ®Google Scholar
• DeLey J., Mannheim W., Segers P., Lievens A., Denijn M., Vanhouke M., Gillis M. Ribosomal ribonucleic acid cistron similarities and taxonomic neighborhood of Brucella and CDC group Vd. Int. J. Syst. Bacteriol. 1988; 37: 35
   Google Scholar
• O'Hara M. J., Collins D. M., DeLisle G. W. Restriction endonuclease analysis of Brucella ovis and other Brucella species. Vet. Microbiol. 1985; 10: 425
   PubMed Web of Science ®Google Scholar
• Bundle D. R., Cherwonogrodzky J. W., Perry M. B. Structural elucidation of the Brucella melitensis M antigen by high-resolution NMR at 500 MHz. Biochemistry 1987; 26: 8717
   PubMed Web of Science ®Google Scholar
• Wenzel R., Herrmann R. Physical mapping of the Mycoplasma pneumoniae genome. Nucl. Acid. Res. 1988; 16: 8323
   PubMed Web of Science ®Google Scholar
• Joint FAO/WHO Expert Committee on brucellosis. WHO Tech. Rep. Ser. 1986; 1: 740
   Google Scholar
• Ackermann H.-W., Simon F., Verger J. M. A survey of Brucella pages and morphology of new isolates. Intervirology 1981; 16: 1
   PubMed Web of Science ®Google Scholar
• Corbel M. J. Brucella phages: advances in the development of a reliable phage typing system for smooth and non-smooth Brucella isolates. Ann. Inst. Pasteur Microbiol. 1987; 138: 70
   Google Scholar
• Corbel M. J., Tolair F. Characterisation of a new phage lytic for both smooth and non-smooth Brucella species. Res. Vet. Sci. 1988; 44: 45
   PubMed Web of Science ®Google Scholar
• Lindberg A. A., Hellerqvist C. G., Bagdian-Motta G., Makela P. H. Lipopolysaccharide modification accompanying antigenic conversion by phage P27. J. Gen. Microbiol. 1978; 107: 279
   Google Scholar
• Smith I. D., Heffron E. Transposon Tn5 mutagenesis of Brucella abortus. Infect. Immun. 1987; 55: 2774
   PubMed Web of Science ®Google Scholar
• Henry B. S. Dissociation in the genus Brucella. J. Infect. Dis. 1933; 52: 374
   Google Scholar
• Hadley P. Microbic dissociation. J. Infect. Dis. 1927; 40: 1
   Google Scholar
• Frost A. J., Smith H., Witt K., Keppie J. The chemical basis of the virulence of Brucella abortus. X. A surface virulence factor which facilitates intracellular growth of Brucella abortus in bovine phagocytes. Br. J. Exp. Pathol. 1972; 53: 587
   PubMedGoogle Scholar
• Braude A. I. Studies in the pathology and pathogenesis of experimental brucellosis. I. A comparison of the pathogenicity of Brucella abortus, Brucella melitensis and Brucella suis for guinea pigs. J. Infect. Dis. 1951; 89: 76
   PubMed Web of Science ®Google Scholar
• Meyer K. F., Fleischner E. C. The pathogenicity of Brucella melitensis and Brucella abortus for guinea pigs. J. Infect. Dis. 1922; 31: 159
   Google Scholar
• Lory S., Tai P. C. Biochemical and genetic aspects of Pseu-domonas aeruginosa virulence. Curr. Top. Microbiol. Immunol. 1984; 118: 53
   Web of Science ®Google Scholar
• Moreno E., Pitt M. W., Jones L. M., Shurig G. G., Berman D. T. Purification and characterization of smooth and rough lipopolysaccharides from Brucella abortus. J. Bacleriol. 1979; 138: 361
   PubMed Web of Science ®Google Scholar
• Baker P. J., Wilson J. B. Chemical composition and biological properties of endotoxin of Brucella abortus. J. Bacleriol. 1965; 90: 895
   PubMed Web of Science ®Google Scholar
• Baker P. J., Wilson J. B. Hypoferremia in mice and its application to the bioassay of endotoxin. J. Bactenol. 1965; 90: 903
   PubMed Web of Science ®Google Scholar
• Kreutzer D. L., Buller C. S., Robertson D. C. Chemical characterization and biological properties of lipopolysacchandes isolated from smooth and rough strains of Brucella abortus. Infect. Immun. 1979; 23: 811
   PubMed Web of Science ®Google Scholar
• Montaraz J. A., Winter A. J., Hunter D. M., Sowa B. A., Adams L. G. Protection against Brucella abortus in mice with O-polysaccharide-specific monoclonal antibodies. Infect. Immun. 1986; 51: 961
   PubMed Web of Science ®Google Scholar
• Braun W. Bacterial dissociation. Bacleriol. Rev. 1947; 11: 75
   PubMedGoogle Scholar
• Goodlow R. J., Tucker L., Braun W., Mika L. A. Effect of the isomenc configuration of the source of nitrogen on changes in population and metabolism in cultures of Brucella. J. Bacleriol. 1952; 63: 681
   PubMed Web of Science ®Google Scholar
• Goodlow R. J., Braun W., Mika L. A. The role of D-alamne in the growth and variation of Brucella abortus. Arch. Biochem. 1951; 30: 402
   PubMedGoogle Scholar
• Kreutzer D. L., Robertson D. C. Surface macromolecules and virulence in intracellular parasitism: comparison of cell envelope components of smooth and rough strains of Brucella abortus. Infect. Immun. 1979; 23: 819
   PubMed Web of Science ®Google Scholar
• Plastridge W. N., McAlpine J. G. Microbic dissociation in the abortus-melitensis group. J. Infect. Dis. 1930; 46: 315
   Google Scholar
• Huddleson I. F. The immunization of guinea pigs with mucoid phases of Brucella. Am. J. Vet. Res. 1947; 8: 374
   PubMed Web of Science ®Google Scholar
• Carmichael I. E., Bruner D. W. Characteristics of a newly recognized species of Brucella responsible for infectious canine abortions. Cornell Vet. 1968; 58: 579
   Google Scholar
• Taylor A. W., McDiarmid A. The stability of the avirulent characters of Brucella abortus strain 19 and strain 45/20 in lactating and pregnant cattle. Vet. Rec. 1949; 61: 317
   Google Scholar
• Kleckner N., Chan R., Tye B.-K., Botstein D. Genetic engineering in vivo using translocatable drug-resistance elements. J. Mol. Biol. 1977; 116: 125
   PubMed Web of Science ®Google Scholar
• Naide Y., Nikaido H., Makela P. H., Wilkinson R. G., Stocker B. A. D. Semirough strains of Salmonella. Proc. Natl Acad. Sci. U.S.A. 1965; 53: 147
   PubMed Web of Science ®Google Scholar
• Hatten B. A., Schmitt-Slomska J. Brucella L-forms: their occurrence and characteristics. Bacterial L-Forms, S. Madoff. Marcel Dekker, New York 1986; 163
   Google Scholar
• Huddleson I. F., Richardson M. A., Warner J., Baltzer B. The characteristics and dissociation pattern of type G (microcolony type) of Brucella abortus, in Studies in Brucellosis III. Mich. Agric. Exp. Stn. Mem. 1952; 6: 64
   Google Scholar
• Meyer M. E. Evolution and taxonomy in the genus Brucella: progesterone induction of filterable forms of Brucella abortus biotype 2 with revertant characteristics essentially indistinguishable in vitro from those of Brucella ovis. Am. J. Vet. Res. 1976; 211: 37
   Google Scholar
• Alton G. G., Jones L. M., Pietz D. E. Laboratory techniques in brucellosis. WHO Monogr. Ser. 1975; 55: 11
   Google Scholar
• Caroff M., Bundle D. R., Perry M. B. Structure of the O-chain of the phenol phase soluble cellular lipopolysaccharide of Yersinia enterocolitica serotype O:9. Eur. J. Biochem. 1984; 139: 195
   PubMedGoogle Scholar
• Moreno E., Mayer H., Moriyon I. Characterization of a native polysaccharide hapten from Brucella melitensis. Infect. Immun. 1987; 55: 2850
   PubMed Web of Science ®Google Scholar
• Galanos C., Luderitz O., Rietschel E. T., Westphal O. Biological activities of lipid A complexed with bovine serum albumin. Eur. J. Biochem. 1972; 31: 230
   PubMedGoogle Scholar
• Bundle D. R., Cherwonogrodzky J. W., Perry M. B. Characterization of Brucella polysaccharide B. Infect. Immun. 1988; 56: 1101
   PubMed Web of Science ®Google Scholar
• Smith H., Fitzgeorge R. B. The chemical basis of virulence of Brucella abortus V. The basis of intracellular survival and growth in bovine phagocytes. Br. J. Exp. Pathol. 1964; 45: 174
   PubMedGoogle Scholar
• Riley L. K., Robertson D. C. Brucellacidal activity of human and bovine polymorphonuclear leukocyte granule extracts against smooth and rough strains of Brucella abortus. Infect. Immun. 1984; 46: 231
   PubMed Web of Science ®Google Scholar
• Keppie J., Witt K., Smith H. The chemical basis of virulence of Brucella abortus. DC. The increased immunogenicity of Br. abortus grown in media which enhance its ability to survive within bovine phagocytes. Br. J. Exp. Pathol. 1969; 50: 219
   PubMedGoogle Scholar
• Winter A. J., Howe G. E., Duncan J. R., Els M. J., Widom J., Ganem B., Morein B. Effectiveness of natural and synthetic complexes of porin and O polysaccharide as vaccines against Brucella abortus in mice. Infect. Immun. 1988; 56: 3251
   PubMed Web of Science ®Google Scholar
• Kuusi N., Nurminen M., Saxen H., Makela P. H. Immunization with major outer membrane protein (porin) preparations in experimental murine salmonellosis: effect of lipopolysaccharide. Infect. Immun. 1981; 34: 328
   PubMed Web of Science ®Google Scholar
• Adams I. G., unpublished observations
   Google Scholar
• McKeon F. W. A recent trial comparing two 45/20 adjuvant vaccines, Int. Symp. on Brucellosis II. Dev. Biol. Stand. 1976; 31: 343
   PubMedGoogle Scholar
• Isibasi A., Ortiz V., Vargas M., Paniagua J., Gonzalez C., Moreno J., Kumate J. Protection against Salmonella typhi infection in mice after immunization with outer membrane proteins isolated from Salmonella typhi 9, 12, d, Vi. Infect. Immun. 1988; 56: 2953
   PubMed Web of Science ®Google Scholar
• Verstreate D. R., Creasy M. T., Caveney N. T., Baldwin C. L., Blau M. W., Winter A. J. Outer membrane proteins of Brucella abortus: isolation and characterization. Infect. Immun. 1982; 35: 979
   PubMed Web of Science ®Google Scholar
• Santos J. M., Verstreate D. R., Perera V. Y., Winter A. J. Outer membrane proteins from rough strains of four Brucella species. Infect. Immun. 1984; 34: 1000
   Google Scholar
• Douglas J. T., Rosenberg E. Y., Nikaido H., Verstreate D. R., Winter A. J. Porins of Brucella species. Infect. Immun. 1984; 44: 37
   Web of Science ®Google Scholar
• Chen R., Schmidmayr W., Kramer C., Chen-Schmeisser V., Henning U. Primary structure of major outer membrane protein II* (OmpA protein) of Escherichia coli K-12. Proc. Natl. Acad. Sci. U.S.A. 1980; 77: 4592
   PubMed Web of Science ®Google Scholar
• Gomez-Miguel M. J., Moriyon I. Demonstration of a peptid-oglycan-linked lipoprotein and characterization of its trypsin fragment in the outer membrane of Brucella spp. Infect. Immun. 1986; 53: 678
   PubMed Web of Science ®Google Scholar
• Gomez-Miguel M. J., Moriyon I., Lopez J. Brucella outer membrane lipoprotein shares antigenic determinants with Escherichia coli, Braun lipoprotein and is exposed on the cell surface. Infect. Immun. 1987; 55: 258
   PubMed Web of Science ®Google Scholar
• Mayfield J. E., Bricker B. B., Godfrey H., Crosby R. M., Knight D. J., Hailing S. M., Balinsky D., Tabatabai L. B. The cloning, expression, and nucleotidc sequence of a gene coding for an immunogenic Brucella abortus protein. Gene 1988; 63: 1
   PubMed Web of Science ®Google Scholar
• Young R., Davis R. W. Efficient isolation of genes using antibody probes. Proc. Natl. Acad. Sci. U.S.A. 1983; 80: 1194
   PubMed Web of Science ®Google Scholar
• Benson S. A., Occi J. L. L., Sampson B. A. Mutations that alter the pore function of the OmpF porin of Escherichia coli K12. J. Mol. Biol. 1988; 203: 961
   PubMed Web of Science ®Google Scholar
• Wang L. I., Frash C. E. Development of a Neisseria menin-gitidis group B serotype 2b protein vaccine and evaluation in a mouse model. Infect. Immun. 1984; 46: 408
   PubMed Web of Science ®Google Scholar
• Afzal M., Brodie S. J., Tengerdy R. P., Squire P. G. Isolation and antigenic activity of Brucella ovis outer membrane proteins. J. Clin. Microbiol 1987; 25: 2132
   PubMed Web of Science ®Google Scholar
• Baldwin C. L., Verstreate D. R., Winter A. J. Immune response of cattle to Brucella abortus outer membrane proteins measured by lymphocyte blastogenesis. Vet. Immun. Immunopathol. 1985; 9: 383
   PubMed Web of Science ®Google Scholar
• Adams L. G., Crawford R. P., Ficht T. A., Smith R., III., Sowa B. A., Templeton J. W., Williams J. D., Wu A. M. New approaches for vaccinating against bovine brucellosis. 40th Annu. Brucellosis Conf., Abstract, Chicago, 1987
   Google Scholar
• Stinebring W. R., Braun W., Pomales-Lebron A. Modified serum resistance of bacteria following intracellular residence. Ann. N.Y. Acad. Sci. 1960; 88: 1230
   Web of Science ®Google Scholar
• Nielsen K. Cleavage of bovine immunoglobulin G* in whey by an extracellular material from Brucella abortus. Can. J. Comp. Med. 1985; 49: 337
   PubMedGoogle Scholar
• Huddleson I. F., Stahl W. H. Catalase activity of the species of Brucella as a criterion of virulence, in Studies in Brucellosis II. Mich. Agric. Exp. Stn. Tech. Bull. 1943; 182: 57
   Google Scholar
• Wilson J. B., Dasinger B. L. Biochemical properties of virulent and avirulent strains of Brucellae. Ann. N.Y. Acad. Sci. 1960; 88: 1155
   PubMed Web of Science ®Google Scholar
• Hart D. A. P., Armstrong J. A., Brown C. A., Draper P. Ultrastructural study of the behavior of macrophages toward parasitic mycobacteria. Infect. Immun. 1972; 5: 803
   PubMed Web of Science ®Google Scholar
• Carroll M. E. W., Jackett P. S., Aber V. R., Lowrie D. B. Phagolysosome formation, cyclic adenosine 3′:5′- monophos-phate and the fate of Salmonella typhimurium within mouse peritoneal macrophages. J. Gen. Microbiol. 1979; 110: 421
   PubMedGoogle Scholar
• Klebanoff S. J. Antimicrobial leukocytes. Semin. Hematol 1975; 12: 117
   PubMed Web of Science ®Google Scholar
• Spitznagel J. K. Oxygen-independent antimicrobial systems in polymorphonuclear leukocytes. The Reticuloendothelial System: A Comprehensive Treatise. Biochemistry and Metabolism, A. J. Sbarra, R. Strauss. Plenum Press, New York 1980; 355
   Google Scholar
• Goren M. N., Hart D. A. P., Young M. R., Armstrong J. R. Prevention of phagosome-lysosome fusion in cultured macrophages by sulfatides of Mycobacterium tuberculosis. Proc. Natl. Acad. Sci. U.S.A. 1976; 73: 2510
   PubMedGoogle Scholar
• Lowrie D. B., Jackett P. S., Ratcliffe N. A. Mycobacterium microti may protect itself from intracellular destruction by releasing cyclic AMP into phagosomes. Nature 1975; 254: 600
   PubMed Web of Science ®Google Scholar
• Weissman G., Zurier R. B., Hoffstein S. Leukocytic proteases and the immunologic release of lysosomal enzymes. Am. J. Pathol. 1972; 68: 539
   PubMed Web of Science ®Google Scholar
• Oberti J., Caravano R., Roux R. Essai de determination quantitative de la fusion phagolysosomiale au cours de l'infection de macrophages murins par Brucella suis. Ann. Immunol. (Inst. Pasteur) 1981; 132D: 201
   Google Scholar
• Morris J. A. The interaction of Brucella abortus 544 and neutrophil polymorphonuclear leukocytes. Ann. Sclavo 1977; 19: 143
   PubMedGoogle Scholar
• Barrett J. T. Textbook of Immunology, 3rd ed. C. V. Mosby, St Louis 1978; 261
   Google Scholar
• McEwen A. D. Experiments on contagious abortion. The immunity of cattle inoculated with vaccines of graded virulence. Vet. Rec. 1940; 52: 815
   Google Scholar
• Edwards S. J., DeRopp R. A., McLeod D. H. A study of the immunological properties and infectivity of Brucella abortus strain 45/20, McEwen, in cattle. Vet. Rec. 1945; 57: 259
   Google Scholar
• Alton G. G. Experiences with Brucella vaccines. Bovine Brucellosis, An International Symposium, R. P. Crawford, R. J. Hidalgo. Texas A & M University Press, College Station 1977; 209
   Google Scholar
• DeChatelet L. R. Oxidative bactericidal mechanisms of polymorphonuclear leukocytes. J. Infect. Dis. 1975; 131: 295
   PubMed Web of Science ®Google Scholar
• Robertson D. C., McCullough W. G. The glucose catabolism of the genus Brucella. I. Evaluation of pathways. Arch. Biochem. Biophys 1968; 127: 263
   PubMed Web of Science ®Google Scholar
• Robertson D. C., McCullough W. G. The glucose catabolism of the genus Brucella. II. Cell-free studies with B. abortus (S-19). Arch. Biochem. Biophys. 1968; 127: 445
   PubMed Web of Science ®Google Scholar
• Frenchick P. J., Markham R. J. F., Cochrane A. H. Inhibition of phagosome-lysosome fusion in macrophages by soluble extracts of virulent Brucella abortus. Am. J. Vet. Res. 1985; 46: 332
   PubMed Web of Science ®Google Scholar
• Lowrie D. B., Aber V. R., Jackett P. S. Phagosome-lysosome fusion and cyclic adenosine 3′:5′-monophosphate in macrophages infected with Mycobacterium microti, Mycobacterium bovis BCG or Mycobacterium lepraemurium. J. Gen. Microbiol. 1979; 110: 431
   PubMedGoogle Scholar
• Muchmore A. V., Decker J. M., Blaese R. M. Evidence that specific oligosaccharides block early events necessary for the expression of antigen-specific proliferation by human lymphocytes. J. Immunol. 1980; 125: 1306
   PubMed Web of Science ®Google Scholar
• Canning P. C., Roth J. A., Tabatabai L. B., Deyoe B. L. Isolation of components of Brucella abortus responsible for inhibition of function in bovine neutrophils. J. Infect. Dis. 1985; 152: 913
   PubMed Web of Science ®Google Scholar
• Bertram T. A., Canning P. A., Roth J. A. Preferential inhibition of primary granule release from bovine neutrophils by a Brucella abortus extract. Infect. Immun. 1986; 52: 285
   PubMed Web of Science ®Google Scholar
• Canning P. C., Roth J. A., Deyoe B. L. Release of 5′-guanosine monophosphate and adenine by Brucella abortus and their role in the intracellular survival of the bacteria. J. Infect. Dis. 1986; 154: 464
   PubMed Web of Science ®Google Scholar
• Ignarro L. J. Regulation of lysosomal enzyme release by prosta-glandins, autonomic neurohormones and cyclic nucleotides. Lyso-somes in Biology and Pathology, J. T. Dingle, R. T. Dean. North-Holland, Amsterdam 1975; 4: 481
   Google Scholar
• Weismann G., Goldstein I., Hoffstein S., Chauvet G., Ro-bineaux R. Yin/Yang modulation of lysosomal enzyme release from polymorphonuclear leukocytes by cyclic nucleotides. Ann. N.Y. Acad. Sci. 1975; 256: 222
   PubMed Web of Science ®Google Scholar
• Pearce J. H., Williams A. E., Harris-Smith P. W., Fitzgeorge R. B., Smith H. The chemical basis of the virulence of Brucella abortus. II. Erythritol, a constituent of bovine foetal fluids which stimulates the growth of Br. abortus in bovine phagocytes. Br. J. Exp. Pathol. 1962; 43: 31
   Google Scholar
• Williams A. E., Keppie J., Smith H. The chemical basis of the virulence of Brucella abortus. III. Foetal erythritol a cause of the localisation of Brucella abortus in pregnant cows. Br. J. Exp. Pathol. 1962; 43: 530
   PubMedGoogle Scholar
• Slotnick I. J., Dougherty M. Erythritol as a selective substrate for growth of Serratia marcescens. Appl. Microbiol. 1972; 24: 292
   PubMedGoogle Scholar
• Wawszkiewicz E. J., Barker H. A. Erythritol metabolism by Propionibacterium pentosaceum. J. Biol. Chem. 1948; 243, 1968
   PubMed Web of Science ®Google Scholar
• Jakoby W. B., Fredericks J. Erythritol dehydrogenase from Aerobacter aerogenes. Biochim. Biophys. Acta 1961; 48: 26
   PubMedGoogle Scholar
• Whistler R. L., Underkofler L. A. The production of l-ery-thrulose by the action of Acetobacter suboxydans upon erythntol. J. Am. Chem. Soc. 1938; 60: 2507
   Google Scholar
• Hiatt H. H., Horecker B. L. D-Erythrose metabolism in a strain of Alcaligenes faecalis. J. Bacteriol. 1956; 71: 649
   PubMed Web of Science ®Google Scholar
• Braun M. L., Niederpreum D. J. Erythritol metabolism in wild-type and mutant strains of Schizophyllum commune. J. Bacteriol. 1969; 100: 625
   PubMed Web of Science ®Google Scholar
• Sperry J. A., Robertson D. C. Erythritol catabolism by Brucella abortus. J. Bacteriol. 1975; 121: 619
   PubMed Web of Science ®Google Scholar
• Holten D., Fromm H. J. Purification and properties of erythntol kinase from Propionibacterium pentosaceum. J. Biol. Chem. 1961; 236: 2581
   PubMed Web of Science ®Google Scholar
• Sperry J. F., Robertson D. C. Inhibition of growth by erythritol catabolism in Brucella abortus. J. Bacteriol. 1975; 124: 391
   PubMed Web of Science ®Google Scholar
• McCorkindale J., Edson N. L. Polyol Dehydrogenases 1. The specificity of rat-liver polyol dehydrogenase. Biochem. J. 1854; 57: 518
   Google Scholar
• Hickman J., Ashwell G. A sensitive and stereospecific enzymatic assay for xylulose. J. Biol. Chem. 1959; 234: 758
   PubMed Web of Science ®Google Scholar
• Harold F. M. Conservation and transformation of energy by bacterial membranes. Bacteriol. Rev. 1972; 36: 172
   PubMedGoogle Scholar
• Touster O., Hecht S. O., Todd W. M. The isolation of crystalline erythritol from normal human urine. J. Biol. Chem. 1960; 235: 951
   PubMed Web of Science ®Google Scholar
• Meyer M. E. Metabolic charactenzation of the genus Brucella, V. Relationship of strain oxidation rate of i-erythritol to strain virulence for Guinea pigs. J. Bacteriol. 1966; 92: 584
   PubMed Web of Science ®Google Scholar