Avian antimicrobial proteins: structure, distribution and activity

References

• AGUILERA, O., QUIROS, L.M. and FIERRO, J.F. (2003) Transferrins selectively cause ion efflux through bacterial and artificial membranes. FEBS Letter 548: 5–10.
   PubMed Web of Science ®Google Scholar
• ANDREU, D. and RIVAS, L. (1998) Animal antimicrobial peptides: an overview. Biopolymers 47: 415–433.
   PubMed Web of Science ®Google Scholar
• BANDYOPADHYAY, A. and BHATTACHARYYA, S.P. (1996) Influence of fowl uropygial gland and its secretory lipid components on growth of skin surface bacteria of fowl. Indian Journal of Experimental Biology 34(1): 48–52.
   PubMedGoogle Scholar
• BANDYOPADHYAY, A. and BHATTACHARYYA, S.P. (1999) Influence of fowl uropygial gland and its secretory lipid components on the growth of skin surface fungi of fowl. Indian Journal of Experimental Biology 37(12): 1218–1222.
   PubMedGoogle Scholar
• BERA, A., HERBERT, S., JAKOB, A., VOLLMER, W. and GOTZ, F. (2005) Why are pathogenic staphylococci so lysozyme resistant? The peptidoglycan O-acetyltransferase OatA is the major determinant for lysozyme resistance of Staphylococcus aureus. Molecular Microbiology 55(3): 778–787.
   PubMed Web of Science ®Google Scholar
• BIRK, Y., KHALEF, S. and JIBSON, M.D. (1983) Purification and properties of protease F, a bacterial enzyme with chymotrypsin and elastase specificities. Archives of Biochemistry and Biophysics 225(2): 451–457.
   PubMed Web of Science ®Google Scholar
• BROCKUS, C.W., JACKWOOD, M.W. and HARMON, B.G. (1998) Characterisation of β-defensin prepropeptide mRNA from chicken and turkey bone marrow. Animal Genetics 29: 283–289.
   PubMed Web of Science ®Google Scholar
• BROQUIST, H.P. and SNELL, E.E. (1951) Biotin and bacterial growth. Relation to aspartate, oleata and carbon dioxide. Journal of Biological Chemistry 188(1): 431–444.
   PubMed Web of Science ®Google Scholar
• BULET, P., STOCKLIN, R. and MENIN, L. (2004) Anti-microbial peptides: from invertebrates to vertebrates. Immunological Reviews 198: 169–184.
   PubMed Web of Science ®Google Scholar
• BURLEY, R.W. and VADEHRA, D.V. (1989) The avian egg chemistry and biology. John Wiley and Sons Inc, New York.
   Google Scholar
• CANFIELD, R.E. and MCMURRY, S. (1967) Purification and characterisation of a lysozyme from goose egg white. Biochemical and Biophysical research communications 26: 38–42.
   PubMed Web of Science ®Google Scholar
• DAVIES, E.A., BEVIS, H.E. and DELVES-BROUGHTON, J. (1997) The use of the bacteriocin, nisin, as a preservative in ricotta-type cheeses to control the food-borne pathogen Listeria monocytogenes. Letters in Applied Microbiology 24: 343–346.
   PubMed Web of Science ®Google Scholar
• DIANOUX, A-C. and JOLLES, P. (1967) A study of a lysozyme poor in cystine and tryptophan: the lysozyme of goose egg white. Biochimical et Biophysical Acta 133(3): 472–479.
   PubMed Web of Science ®Google Scholar
• DEEMING, D.C. (1987) Effect of cuticle removal on the water vapour conductance of egg shells of several species of domestic bird. British Poultry Science 28: 231–237.
   Web of Science ®Google Scholar
• EVANS, E.W., BEACH, G.G., WUNDERLICH, J. and HARMON, B.G. (1994) Isolation of antimicrobial peptides from avian heterophils. Journal of Leukocyte Biology 56: 661–665.
   PubMed Web of Science ®Google Scholar
• EVANS, E.W., BEACH, G.G., MOORE, K.M., JACKWOOD, M.W., GLISSON, J.R. and HARMON, B.G. (1995) Antimicrobial activity of chicken and turkey heterophil peptides CHP1, CHP2, THP1 and THP3. Veterinary Microbiology 47: 295–303.
   PubMed Web of Science ®Google Scholar
• FLORKIN, M., SCHEER, B.T. and BRUSH, A.H. (1978) Chemical zoology. Volume 10. Aves. Academic Press, New York, 436p.
   Google Scholar
• GANZ, T. (2003) Defensins: antimicrobial peptides of innate immunity. Nature Reviews Immunology 3(9): 710–720.
   PubMed Web of Science ®Google Scholar
• GAUTRON, J., HINCKE, M.T., PANHELEUX, M., BAIN, M., MCKEE, M.D., SOLOMON, S.E. and NYS, Y. (2001) Ovocalyxin-32, a novel chicken eggshell matrix protein. Isolation, amino acid sequencing, cloning, and immunocytochemical localization. Journal of Biological Chemistry 276(42): 39243–39252.
   PubMed Web of Science ®Google Scholar
• GAUTRON, J., MURAYAMA, E., VIGNAL, A., MORISSON, M., MCKEE, M.D., REHAULT, S., VIDAL, M.L., NYS, Y. and HINCKE, M.T. (2007) Cloning of ovocalyxin-36, a novel chicken eggshell protein related to lipopolysaccharide-binding proteins (LPB) bactericidal permeability-increasing proteins (BPI), and Plunc family proteins. Journal of Biological Chemistry 282(8): 5273–5286.
   PubMed Web of Science ®Google Scholar
• GIANSANTI, F., ROSSI, P., MASSUCCI, M. T., BOTTI, D., ANTONINI, G., VALENTI, P. and SEGANTI, L. (2002) Antiviral activity of ovotransferrin discloses an evolutionary strategy for the defensive activities of lactoferrin. Biochemistry and Cell Biology 80: 125–130.
   PubMed Web of Science ®Google Scholar
• GRAHAM, I. and WILLIAMS, J. (1975) A comparison of glycopeptides from the transferrins of several species. Biochemical Journal 145: 263–279.
   PubMed Web of Science ®Google Scholar
• GREENGARD, O., SENTENAC, A. and MENDELSOHN, N. (1964) Phosvitin, the iron carrier of egg yolk. Biochimica et Biophysica Acta 90: 406–407.
   PubMed Web of Science ®Google Scholar
• GUERIN-DUBIARD, C., PASCO, M., MOLLE, D., DESERT, C., CROGUENNEC, T. and NAU, F. (2006) Proteomic analysis of hen egg white. Journal of Agricultural and Food Chemistry 54: 3901–3910.
   PubMed Web of Science ®Google Scholar
• HARMON, B.G. (1998) Avian heterophils in inflammation and disease resistance. Poultry Science 77: 972–977.
   PubMed Web of Science ®Google Scholar
• HANCOCK, R.E.W. and CHAPPLE, D.S. (1999) Peptide Antibiotics. Antimicrobial Agents and Chemotherapy 43(6): 1317–1323.
   PubMed Web of Science ®Google Scholar
• HARWIG, S.S.L., SWIDEREK, K.M., KOKRYAKOV, V.N., TAN, L., LEE, T.D., PANYUTICH, E.A., ALESHINA, G.A., SHAMOVA, O.V. and LEHRER, R.I. (1994) Gallinacins: cysteine-rich antimicrobial peptides of chicken leukocytes. FEBS Letters 342: 281–285.
   PubMed Web of Science ®Google Scholar
• HEMMEN, F., MAHANA, W., JOLLES, P. and PARAF, A. (1992) Common antigenic properties of a g-type (goose) and a c-type (duck) egg white lysozyme: antibody response in rabbits and mice. Experientia 48: 79–84.
   PubMedGoogle Scholar
• HERMANN, J., JOLLES, J. and JOLLES, P. (1971) Multiple forms of duck-egg white lysozyme. Primary structure of two duck lysozymes. European Journal of Biochemistry 24(1): 12–17.
   PubMedGoogle Scholar
• HIGGS, R., LYNN, D.J., GAINES, S., MCMAHON, J., TIERNEY, J., JAMES, T., LLOYD, A.T., MULCAHY, G. and O'FARRELLY, C. (2005) The synthetic form of a novel chicken β-defensin identified in silico is predominantly active against intestinal pathogens. Immunogenetics 57: 90–98.
   PubMed Web of Science ®Google Scholar
• HINCKE, M.T., GAUTRON, J., PANHELEUX, M., GARCIA-RUIZ, J., MCKEE, M.D. and NYS, Y. (2000) Identification and localization of lysozyme as a component of eggshell membranes and eggshell matrix. Matrix Biology 19: 443–453.
   PubMed Web of Science ®Google Scholar
• HINCKE, M.T., GAUTRON, J., MANN, K., PANHÉLEUX, M., MCKEE, M.D., BAIN, M., SOLOMON, S.E. and NYS, Y. (2003) Purification of ovocalyxin-32, a novel chicken eggshell matrix protein. Connective Tissue Research 44(suppl. 1): 16–19.
   PubMed Web of Science ®Google Scholar
• HINDENBURG, A., SPITZNAGEL, J. and ARNHEIM, N. (1974) Isozymes of lysozyme in leukocytes and egg white: evidence for the species-species control of egg-white lysozyme synthesis. Proceedings of the National Academy of Science 71(5): 1653–1657.
   PubMed Web of Science ®Google Scholar
• HUMPHREY, T.J. and WHITEHEAD, A. (1993) Egg age and the growth of Salmonella enteritidis PT4 in egg contents. Epidemiology and Infection 111(2): 209–219.
   PubMed Web of Science ®Google Scholar
• HUMPHREY, T.J., WHITEHEAD, A., GAWLER, A.H., HENLEY, A. and ROWE, B. (1991) Numbers of Salmonella enteritidis in the contents of naturally contaminated hen's eggs. Epidemiology and Infection 106(3): 489–496.
   PubMed Web of Science ®Google Scholar
• IBRAHIM, H.R., HIGASHIGUCHI, S., JUNEJA, L.R., KIM, M. and YAMAMOTO, T. (1996) A structural phase of heat-denatured lysozyme with novel antimicrobial action. Journal of Agriculture and Food Chemistry 44: 1416–1423.
   Web of Science ®Google Scholar
• IBRAHIM, H.R., IWAMORI, E., SUGIMOTO, Y. and AOKI, T. (1998) Identification of a distinct antibacterial domain within the N-lobe of ovotransferrin. Biochimica et Biophysica Acta 1401: 289–303.
   PubMed Web of Science ®Google Scholar
• IBRAHIM, H.R., SUGIMOTO, Y. and AOKI, T. (2000) Ovotransferrin antimicrobial peptide (OTAP-92) kills bacteria through a membrane damage mechanism. Biochimica et Biophysica Acta 1523: 196–205.
   PubMed Web of Science ®Google Scholar
• IBRAHIM, H.R., MATSUZAKI, T. and AOKI, T. (2001a) Genetic evidence that antibacterial activity of lysozyme is independent of its catalytic function. FEBS Letters 506: 27–32.
   PubMed Web of Science ®Google Scholar
• IBRAHIM, H.R., THOMAS, U. and PELLEGRINI, A. (2001b) A helix-loop-helix peptide at the upper lip of the active site cleft of lysozyme confers potent antimicrobial activity with membrane permeabilization action. Journal of Biological Chemistry 276(47): 43767–43774.
   PubMed Web of Science ®Google Scholar
• IRWIN, D.M. and GONG, Z. (2003) Molecular evolution of vertebrate goose-type lysozyme genes. Journal of Molecular Evolution 56: 234–242.
   PubMed Web of Science ®Google Scholar
• KAMYSZ, W. (2005) Are antimicrobial peptides an alternative for conventional antibiotics? Nuclear Medicine Review 8(1): 78–86.
   PubMedGoogle Scholar
• KASSAIFY, Z.G. and MINE, Y. (2004) Effect of food protein supplements on Salmonella enteritidis infection and prevention in laying hens. Poultry Science 83: 753–760.
   PubMed Web of Science ®Google Scholar
• KONDO, K., FUJIO, H. and AMANO, T. (1982) Chemical and immunological properties and amino acid sequences of three lysozymes from Peking-duck egg white. Journal of Biochemistry (Tokyo) 91(2): 571–587.
   PubMed Web of Science ®Google Scholar
• KORANT, B.D., BRZIN, J. and TURK, V. (1985) Cystatin, a protein inhibitor of cysteine proteases alters viral protein cleavages in infected human cells. Biochemical and Biophysical Research Communications 127(3): 1072–1076.
   PubMed Web of Science ®Google Scholar
• LANDON, C., THOUZEAU, C., LABBE, H., BULET, P. and VOVELLE, F. (2004) Solution structure of spheniscin, a β-defensin from the penguin stomach. Journal of Biological Chemistry 279(29): 30422–30439.
   Web of Science ®Google Scholar
• LEE-HUANG, S., HUANG, P.L., SUN, Y., HUANG, P.L., KUMG, H.F., BITHE, D.L. and CHEN, H.C. (1999) Lysozyme RNases as anti-HIV components in beta-core preparations of human chorionic gonadotropin. Proceedings of the National Academy of Sciences of the United States of America 96: 2678–2681.
   PubMed Web of Science ®Google Scholar
• LESNIEROWSKI, G., CEGIELSKA-RADZIEJEWSKA, R. and KIJOWSKI, J. (2004) Thermally and chemical-thermally modified lysozyme and its bacteriostatic activity. World's Poultry Science Journal 60: 303–309.
   Web of Science ®Google Scholar
• LYNN, D.J., HIGGS, R., GAINES, S., TIERNEY, J., JAMES, T., LLOYD, A.T., FARES, M.A., MULCAHY, G. and O'FARRELLY, C. (2004) Bioinformatics discovery and initial characterisation of nine novel antimicrobial peptide genes in the chicken. Immunogenetics 56: 170–177.
   PubMed Web of Science ®Google Scholar
• LYNN, D.J., HIGGS, R., LLOYD, A.T., O'FARRELLY, C., HERVE-GREPINET, V., NYS, Y., BRINKMAN, F.S., YU, P.L., SOULIER, A., KAISER, P., ZHANG, G. and LEHRER, R.I. (2007) Avian beta-defensin nomenclature: a community proposed update. Immunology Letters 110(1): 86–9.
   PubMed Web of Science ®Google Scholar
• MANN, K., MACEK, B. and OLSEN, J. (2006) Proteomic analysis of the acid-soluble organic matrix of the chicken calcified eggshell layer. Proteomics 6: 3801–3810.
   PubMed Web of Science ®Google Scholar
• MARTENS, J-H., BARG, H., WARREN, M.J. and JAHN, D. (2002) Microbial production of vitamin B12. Applied Microbiology and Biotechnology 58: 275–285.
   PubMed Web of Science ®Google Scholar
• MARTIN-PLATERO, A.M., VALDIVIA, E., RUIZ-RODRIGUEZ, M., SOLER, J.J., MARTIN-VIVALDI, M., MAQUEDA, M. and MARTINEZ-BUENO, M. (2006) Characterization of antimicrobial substances produced by Enterococcus faecalis MRR 10–3, isolated from the uropygial gland of the hoopoe (Upupoe epops). Applied and Environmental Microbiology 72(6): 4245–4249.
   PubMed Web of Science ®Google Scholar
• MATSUZAKI, K. (2001) Why and how are peptide-lipid interactions utilized for self defence? Biochemical Society Transactions 29(4): 598–601.
   PubMed Web of Science ®Google Scholar
• MINE, Y., OBERLE, C. and KASSAIFY, Z. (2003) Eggshell matrix proteins as defense mechanism of avian eggs. Journal of Agriculture and Food Chemistry 51(1): 249–253.
   PubMed Web of Science ®Google Scholar
• MINE, Y., MA, F. and LAURIAU, S. (2004) Antimicrobial peptides released by enzymatic hydrolysis of hen egg white lysozyme. Journal of Agricultural and Food Chemistry 52: 1088–1094.
   PubMed Web of Science ®Google Scholar
• MIYAGAWA, S., MATSUMOTO, K., KAMATA, R., OKAMURA, R. and MAEDA, H. (1991a) Spreading of Serratia marcescens in experimental keratitis and growth suppression by chicken egg white ovomacroglobulin. Japanese Journal of Ophthalmology 35(4): 402–410.
   PubMed Web of Science ®Google Scholar
• MIYAGAWA, S., KAMATA, R., MATSUMOTO, K., OKAMURA, R. and MAEDA, H. (1991b) Inhibitory effects of ovomacroglobulin on bacterial kerititis in rabbits. Graefe's Archive for Clinical and Experimental Opthalmology 229(3): 281–286.
   PubMed Web of Science ®Google Scholar
• MOLLA, A., MATSUMURA, Y., YAMAMOTO, T., OKAMURA, R. and MAEDA, H. (1987) Pathogenic capacity of proteases from Serratia marcescens and Pseudomonas aeruginosa and their suppression by chicken egg white ovomacroglobulin. Infection and Immunity 55(10): 2509–2517.
   PubMed Web of Science ®Google Scholar
• MUNIYAPPA, K. and ADIGA, P.R. (1979) Isolation and characterization of thiamine-binding protein chicken egg white. Biochemistry Journal 177: 887–894.
   PubMed Web of Science ®Google Scholar
• NAKANO, T. and GRAF, T. (1991) Goose-type lysozyme gene of the chicken: sequence, genomic organisation and expression reveals major differences to chicken-type lysozyme gene. Biochimica et Biophysica Acta 1090: 273–276.
   PubMed Web of Science ®Google Scholar
• NAKIMBUGWE, D., MASSCHALCK, B., ATANASSOVA, M., ZEWDIE-BOSUNER, A. and MICHIELS, C.W. (2006) Comparison of bactericidal activity of six lysozymes at atmospheric pressure and under high hydrostatic pressure. International Journal of Food Microbiology 108(3): 355–363.
   PubMed Web of Science ®Google Scholar
• NILE, C.J., TOWNES, C.L., HIRST, B.H. and HALL, J. (2006) The novel avian protein, AWAK, contains multiple domains with homology to protease inhibitory modules. Molecular Immunology 43: 388–394.
   PubMed Web of Science ®Google Scholar
• OHASHI, H., SUBEDI, K., NISHIBORI, M., ISOBE, N. and YOSHIMURA, Y. (2005) Expressions of antimicrobial peptide gallinacin-1,-2 and -3 mRNA in the oviduct of laying hens. The Journal of Poultry Science 42: 337–345.
   Google Scholar
• PELLEGRINI, A., HULSMEIER, A.J., HUNZIKER, P. and THOMAS, U. (2004) Proteolytic fragments of ovalbumin display antimicrobial activity. Biochimica et Biophysica Acta 1672: 76–85.
   PubMed Web of Science ®Google Scholar
• PHELPS, C.F. and ANTONINI, E. (1975) A study of the kinetics of iron and copper binding to hen ovotransferrin. Biochemical Journal 147: 385–391.
   PubMed Web of Science ®Google Scholar
• POOART, J., TORIKATA, T. and ARAKI, T. (2004) The primary structure of a novel goose-type lysozyme from rhea egg white. Bioscience Biotechnology and Biochemistry 68(1): 159–169.
   PubMed Web of Science ®Google Scholar
• POOART, J., TORIKATA, T. and ARAKI, T. (2005) Enzymatic properties of rhea lysozyme. Bioscience Biotechnology and Biochemistry 69(1): 103–112.
   PubMed Web of Science ®Google Scholar
• PRAGER, E.M. and JOLLES, P. (1996) Animal lysozymes c and g: an overview. EXS 75: 9–31.
   PubMedGoogle Scholar
• PRAGER, E.M. and WILSON, A.C. (1974) Widespread distribution of lysozyme g in egg white of birds. Journal of Biological Chemistry 249(22): 7295–7297.
   PubMed Web of Science ®Google Scholar
• RAMANATHAN, B., DAVIS, E.G., ROSS, C.R. and BLECHA, F. (2002) Cathelicidins: microbicidal activity, mechanisms of action, and roles in innate immunity. Microbes and Infection 4: 361–372.
   PubMed Web of Science ®Google Scholar
• RAWAS, A., MORETON, K., MUIRHEAD, H. and WILLIAMS, J. (1989) Preliminary crystallographic studies on duck ovotransferrin. Journal of Molecular Biology 208: 213–214.
   PubMed Web of Science ®Google Scholar
• READ, R.J., FUJINAGA, M., SIELECKI, A.R. and JAMES, M.N. (1983) Structure of the complex of Streptomyces griseus protease B and the third domain of the turkey ovomucoid inhibitor at 1.8-A resolution. Biochemistry 22(19): 4420–4233.
   PubMed Web of Science ®Google Scholar
• REDDY, K.V.R., ARANHA, C., GUPTA, S.M. and YEDERY, R.D. (2004) Evaluation of antimicrobial peptide nisin as a safe vaginal contraceptive agent in rabbits: in vitro and in vivo studies. Reproduction 128: 117–126.
   PubMed Web of Science ®Google Scholar
• RICHARDS, M.P. (1997) Trace mineral metabolism in the avian embryo. Poultry Science 76: 152–164.
   PubMed Web of Science ®Google Scholar
• ROSE, E.M. and ORLANS, E. (1981) Immunoglobulins in the egg, embryo and young chick. Developmental and Comparative Immunology 5(1): 15–20.
   PubMed Web of Science ®Google Scholar
• ROSE, E.M., ORLANS, E. and BUTTRESS, N. (1974) Immunoglobulin classes in the hen's egg: their segregation in yolk and white. European Journal of Immunology 4(7): 521–523.
   PubMed Web of Science ®Google Scholar
• SATTAR KHAN, M.A., NAKAMURA, S., OGAWA, M., AKITA, E., AZAKAMI, H. and KATO, A. (2000) Bactericidal action of egg yolk phosvitin against Escherichia coli under thermal stress. Journal of Agricultural and Food Chemistry 48(5): 1503–1506.
   PubMed Web of Science ®Google Scholar
• SAVA, G. (1996) Pharmacological aspects and therapeutic applications of lysozymes. Experimental Science 75: 433–449.
   Google Scholar
• SEVIOUR, E.M. and BOARD, R.G. (1972) Bacterial growth in albumin taken from the eggs of domestic hens and waterfowl. British Poultry Science 13: 557–575.
   PubMed Web of Science ®Google Scholar
• SHAWKEY, M.D., PILLAI, S.R. and HILL, G.E. (2003) Chemical warfare? Effects of uropygial oil on feather-degrading bacteria. Journal of Avian Biology 34(4): 345–349.
   Web of Science ®Google Scholar
• SHELBURNE, C.E., AN, F.Y., DHOLPE, V., RAMAMOORTHY, A., LOPATIN, D.E. and LANTZ, M.S. (2007) The spectrum of antimicrobial activity of the bacteriocin subtilosin A. Journal of Antimicrobial Chemotherapy 59(2): 297–300.
   PubMed Web of Science ®Google Scholar
• SILPHADUANG, U., HINCKE, M.T., NYS, Y. and MINE, Y. (2006) Antimicrobial proteins in chicken reproductive system. Biochemical and Biophysical Research Communications 340: 648–655.
   PubMed Web of Science ®Google Scholar
• SUGIARTO, H. and YU, P-L. (2004) Avian antimicrobial peptides: the defense role of β-defensins. Biochemical and Biophysical Research Communications 323: 721–727.
   PubMed Web of Science ®Google Scholar
• SUGIARTO, H. and YU, P-L. (2006) Identification of three novel ostricacins: an update on the phylogenetic perspective of β-defensins. International Journal of Antimicrobial Agents 27: 229–235.
   PubMed Web of Science ®Google Scholar
• SUPURAN, C.T., SCOZZAFAVA, A. and CLARE, B.W. (2002) Bacterial Protease Inhibitors. Medical Research Reviews 22: 329–372.
   PubMed Web of Science ®Google Scholar
• TABORSKY, G. (1980) Iron binding by phosvitin and its conformational consequences. Journal of Biological Chemistry 255(7): 2976–2985.
   PubMed Web of Science ®Google Scholar
• TENNESSEN, J.A. (2005) Molecular evolution of animal antimicrobial peptides: widespread moderate positive selection. Journal of Evolutionary Biology 18: 1387–1394.
   PubMed Web of Science ®Google Scholar
• THAMMASIRIRAK, S., TORIKATA, T., TAKAMI, K., MURATA, K. and ARAKI, T. (2001) Purification and characterisation of goose type lysozyme from cassowary (Casuarius casuarius) egg white. Bioscience Biotechnology and Biochemistry 65(3): 584–592.
   PubMed Web of Science ®Google Scholar
• THOUZEAU, C., LE MAHO, Y., FROGET, G., SABATIER, L., LE BOHEC, C., HOFFMANN, J.A. and BULET, P. (2003) Spheniscins, avian β-defensins in preserved stomach contents of the king penguin, Aptenodytes patagonicus. Journal of Biological Chemistry 278(51): 51053–51058.
   PubMed Web of Science ®Google Scholar
• TOWNES, C.L., MICHAILIDIS, G., NILE, C.J. and HALL, J. (2004) Induction of cationic chicken liver-expressed antimicrobial peptide 2 in response to salmonella enterica infection. Infection and Immunity: 6987–6993.
   Google Scholar
• TOWNES, C.L., MILONA, P. and HALL, J. (2006) Characterization of AWAP IV, the C-terminal domain of the avian protein AWAK. Biochemical Society Transactions 34(2): 267–269.
   PubMed Web of Science ®Google Scholar
• TSUGE, Y., SHIMOYAMADA, M. and WATANABE, K. (1996a) Binding of egg white proteins to viruses. Bioscience, Biotechnology and Biochemistry 60: 1503–1504.
   PubMed Web of Science ®Google Scholar
• TSUGE, Y., SHIMOYAMADA, M and WATANABE, K. (1996b) Differences in hemagglutination inhibition activity against bovine rotavirus and hen Newcastle disease virus based on the subunits in hen egg white ovomucin. Bioscience, Biotechnology and Biochemistry 60: 1505–1506.
   PubMed Web of Science ®Google Scholar
• TSUGE, Y., SHIMOYAMADA, M. and WATANABE, K. (1997a) Structural features of Newcastle disease virus- and anti-ovomucin antibody-binding glycopeptides from pronase-treated ovomucin. Journal of Agricultural and Food Chemistry 45: 2393–2398.
   Web of Science ®Google Scholar
• TSUGE, Y., SHIMOYAMADA, M. and WATANABE, K. (1997b) Bindings of ovomucin to Newcastle disease virus and anti-ovomucin antibodies and its heat stability based on binding abilities. Journal of Agricultural and Food Chemistry 45: 4629–4634.
   Web of Science ®Google Scholar
• VALENTI, P., DE STASIO, A., MASTROMERINO, P., SEGANTI, L., SINIBALDI, L. and ORSI, N. (1981a) Influence of bicarbonate and citrate on the bacteriostatic action of ovotransferrin towards staphylococci. FEMS Microbiology Letters 10: 77–79.
   Web of Science ®Google Scholar
• VALENTI, P., GUARINO, M., VISCA, P., VON HUNOLSTEIN, ANTONINI, G., DE STASIO, A. and ORSI, N. (1981b) Resistance of genus proteus to ovotransferrin. Bollettino dell'Istituto sieroterapico Milanese 60(4): 284–287.
   PubMedGoogle Scholar
• VALENTI, P., ANTONINI, G., ROSSI FANELLI, M.R., ORSI, N. and ANTONINI, E. (1982) Antibacterial activity of matrix-bound ovotransferrin. Antimicrobial Agents and Chemotherapy 21(5): 840–841.
   PubMed Web of Science ®Google Scholar
• VALENTI, P., ANTONINI, G., VON HUNOLSTEIN, C., VISCA, P., ORSI, N. and ANTONINI, E. (1983) Studies on the antimicrobial activity of ovotransferrin. International Journal of Tissue Reactions V(1): 97–105.
   Google Scholar
• VALENTI, P., VISCA, P., ANTONINI, G. and ORSI, N. (1985) Antifungal activity of ovotransferrin towards genus candida. Mycopathologia 89: 169–175.
   PubMed Web of Science ®Google Scholar
• VALENTI, P., VISCA, P., ANTONINI, G., ORSI, N. and ANTONINI, E. (1987) The effect of saturation with Zn2+ and other metal ions on the antibacterial activity of ovotransferrin. Medical Microbiology and Immunology 176: 123–130.
   PubMed Web of Science ®Google Scholar
• VAN DIJK, A., VELDHUIZEN, E.J.A., VAN ASTEN, A.J.A.M. and HAAGSMAN, H.P. (2005) CMAP27, a novel chicken cathelicidin-like antimicrobial protein. Veterinary Immunology and Immunopathology 106: 321–327.
   PubMed Web of Science ®Google Scholar
• VON HUNOLSTEIN, C., RICCI, M.L., VALENTI, P. and OREFICI, G. (1992) Lack of activity of transferrins towards streptococcus spp. Medical Microbiology Immunology 181: 351–357.
   PubMed Web of Science ®Google Scholar
• WATANABE, K., YSUGE, Y., SHIMOYAMADA, M., OGAMA, N. and EBINA, T. (1998) Antitumor effects of pronase-treated fragments, glycopeptides, from ovomucin in hen egg white in a double grafted tumor system. Journal of Agriculture and Food Chemistry 46: 3033–3038.
   Web of Science ®Google Scholar
• XIAO, Y., HUGHES, A.L., ANDO, J., MATSUDA, Y., CHENG, J-F., SKINNER-NOBLE, D. and ZHANG, G. (2004) A genome-wide screen identifies a single β-defensin gene cluster in the chicken: implications for the origin and evolution of mammalian defensins. BMC Genomics 5: 56.
   PubMed Web of Science ®Google Scholar
• XIAO, Y., CAI, Y., BOMMINENI, Y.R., FERNANDO, S.C., PRAKASH, O., GILLILAND, S.E. and ZHANG, G. (2006a) Identification and functional characterisation of three chicken cathelicidins with potent antimicrobial activity. Journal of Biological Chemistry 281(5): 2858–2867.
   PubMed Web of Science ®Google Scholar
• XIAO, Y., DAI, H., BOMMINENI, Y.R., SOULAGES, J.L., GONG, Y-X., PRAKASH, O. and ZHANG, G. (2006b) Structure-activity relationships of fowlicidin-1, a cathelicidin antimicrobial peptide in the chicken. FEBS Journal 273: 2581–2593.
   PubMed Web of Science ®Google Scholar
• XING, J., WELLMAN-LABADIE, O., GAUTRON, J. and HINCKE, M.T. (2007) Recombinant eggshell ovocalyxin-32: expression, purification and biological activity of the glutathione S-transferase fusion protein. Comparative Biochemistry and Physiology B 147: 172–177.
   PubMed Web of Science ®Google Scholar
• YU, P-L., CHOUDHURY, S.D. and AHRENS, K. (2001) Purification and characterisation of the antimicrobial peptide, ostricacin. Biotechnology Letters 23: 207–210.
   Web of Science ®Google Scholar
• YOSHIMURA, Y., OHASHI, H., SUBEDI, K., NISHIBORI, M. and ISOBE, N. (2006) Effects of age, egg-laying activity, and salmonella-inoculation on the expressions of gallinacin mRNA in the vagina of the hen oviduct. Journal of Reproduction and Development 52(2): 211–218.
   PubMed Web of Science ®Google Scholar
• ZHAO, C., NGUYEN, T., LIU, L., SACCO, R.E., BROGDEN, K.A. and LEHRER, R.I. (2001) Gallinacin-3, an inducible epithelial β-defensin in the chicken. Infection and Immunity: 2684–2691.
   Google Scholar