51
Views
19
CrossRef citations to date
0
Altmetric
Review

Genetically recombinant antibodies: new therapeutics against candidiasis

&
Pages 233-241 | Published online: 03 Mar 2005

Bibliography

  • CASADEVALL A, SCHARFF MD:Return to the past: the case for antibody-based therapies in infectious diseases. Clin. Infect. Dis. (1995) 21:150–161.
  • •Overall review of history and importance of antibody therapy.
  • MATTHEWS RC, RIGG G,HODGETTS S et al: Preclinical assessment of the efficacy of Mycograb®, a human recombinant antibody against fungal H5P90. Antimicrob. Agents Chemother. (2003) 47:2208–2216.
  • ••Original predinical data on Mycograb.
  • BURNIE J, RIGG G, GREGORY C et al.: Aurograb a human recombinant antibody for the treatment of MRSA infection. American Society for MicrobiologyGenera] Meeting (2002).
  • MARTIN GS, MANNINO DM,EATON S, MOSS M: The epidemiology ofsepsis in the United States from 1979 through 2000. N Engl. Med. (2003) 348:1546–1554.
  • MCNEIL MM, NASH SL, HAJJEH RA et al: Trends in mortality due to invasive mycotic diseases in the United States, 1980-1997. Clin. Infect. Dis. (2001) 33:641–647.
  • KONTOYIANNIS DP, LEWIS RE: Antifungal drug resistance of pathogenic fungi. Lancet (2002) 359:1135–1144.
  • BEKERSKY I, FIELDING RIVI, DRESSLER DE, LEE JW, BUELL DN, WALSH TJ: Plasma protein binding of Amphotericin B and pharmacokinetics of bound versus unbound Amphotericin B after administration of intravenous liposomal Amphotericin B (AmBisome) and Amphotericin B deoxycholate. Antimicrob. Agents Chemother: (2002) 46:834–840.
  • NGUYEN MH, CLANCY CJ, YU VLet al: Do in vitro susceptibility data predict the microbiologic response to amphotericin B? Results of a prospective study of patients with Candida fungemia. I Infect. Dis. (1998) 177:425–430.
  • RICHARDSON MD KM: New perspectives in the diagnosis of systemicfungal infections. Ann. Med. (1999) 31:327–335.
  • MATTHEWS RC, BURNIE JP, TABAQCHALI S: Immunoblot analysis of the serological response in systemic candidosis. Lancet (1984) 2:1415–1418.
  • STROCKBINE NA, LARGEN MT, ZWEIBEL SM, BUCKLEY HR: Identification and molecular weight characterization of antigens from Candida albicans that are recognized by human sera. Infect. Immun. (1984) 43:715–721.
  • AU-YOUNG JK, TROY FA,GOLDSTEIN E: Serologic analysis of antigen-specific reactivity in patients with systemic candidiasis. Diagn. Microbiol Infect. Dis. (1985) 3:419–432.
  • MATTHEWS RC, BURNIE JP, TABAQCHALI S: Isolation of immunodominant antigens from sera of patients with systemic candidiasis and characterization of serological response to Candida albicans. .1. Clin. Microbiol (1987) 25:230–237.
  • NEALE TJ, MUIR JC, DRAKE B: The immunochemical characterisation of circulating immune complex constituents in Candida albicans osteomyelitis by isoelectric focusing, immunoblot and immunoprint. Aust. N41. Med. (1987) 17:201–209.
  • MATTHEWS R, BURNIE J, SMITH D et al.: Candida and AIDS: evidence for protective antibody. Lancet (1988) 2:263–266.
  • PORSIUS JC, VAN VLIET HJ,VAN ZEIJL JH, GOESSENS WH, MICHEL MF: Detection of an antibody response in immunocompetent patients with systemic candidiasis orCandida albicans colonisation. Eur. I Clin. Microbiol Infect. Dis. (1990) 9:352–355.
  • FERREIRA RP, YU B, NIKKI Y, ARMSTRONG D: Detection of Candida antigenuria in disseminated candidiasis immunoblotting. I Clin. Microbiol (1990) 28:1075–1078.
  • PETERSON P, PERHEENTUPA J, KROHN KJE: Detection of candidal antigens in autoimmune polyglandular syndrome type I. Clin. Diagn.Lab. Iminunol (1996) 3:290–294.
  • WEIS C, KAPPE R, SONNTAG HG: Western blot analysis of the immune response to Candida albicans antigens in 391 long-term intensive care patients. Mycoses (1997) 40:153–157.
  • MASON AB, BRANDT ME,BUCKLEY HR: Enolase activity associatedwith a C. albicans cytoplasmic antigen.Yeast (1989) 5:S231–S239.
  • MATTHEWS R, BURNIE J: Cloning of a DNA sequence encoding a major fragment of the 47 kiloDalton stress protein homologue of Candida albicans.FEMS Microbiol Lett. (1989) 51:25–30.
  • PANARETOU B, SINCLAIR K, PRODROMOU C, JOHAL J, PEARL L, PIPER PW: The Hsp90 of Candida albicans can confer Hsp90 functions in Saccharomyces cerevisiae: a potential model for the processes that generate immunogenic fragments of this molecular chaperone in C. albicans infections. Microbiology (1999) 145:3455–3463.
  • SWOBODA RK, BERTRAM G,BUDGE S, GOODAY GW, GOW NAR, BROWN AJP: Structure and regulation of the HSP90 gene from the pathogenic fungus Candida albicans. Infect. Iminun. (1995) 63:4506–4514.
  • FRANKLYN KM, WARMINGTON JR: The expression of Candida albicans enolase is not heat shock inducible. FEMS Microbiol Lett. (1994) 118:219–225.
  • BURT ET, O& CONNOR C, LARSEN B: Isolation and identification of a 92-kDa stress induced protein fromCandida albicans. Mycopathologia (1999) 147:13–20.
  • NATHAN DF, LINDQUIST S: Mutational analysis of Hsp90 functions: interactions with a steroid receptor and a protein kinase. Ma Cell. Biol. (1995) 15:3917–3925.
  • NATHAN DF, VOS MH, LINDQUIST S: In vivo functions of theSaccharomyces cerevisiae Hsp90 chaperone. Proc. Nat] Acad. Sci. USA (1997) 25:12949–12956.
  • HOD GETTS S, MATTHEWS R, MORRISSEY G, MITSUTAKE K, PIPER P, BURNIE J: Over-expression of Saccharomyces cerevisiae hsp90 enhances the virulence of this yeast in mice.FEMS Iminunol Med. Microbiol (1996) 31:229–234.
  • ZHANG K, ESSMANN M, BURT ET, LARSEN B: Estrogen effects onCandida albicans: a potential virulence-regulating mechanism. J. Infect. Dis. (1999) 181:1441–1446.
  • MALLOY PJ, ZHAO X, MADANI ND, FELDMAN D: Cloning and expression of the gene from Candida albicans that encodes a high-affinity corticosteroid-binding protein. Proc. Nat] Acad. Sci. USA (1993) 90:1902–1906.
  • DEEGENAARS ML, WATSON K: Stress proteins and stress tolerance in an Antarctic, psychrophilic yeast, Candida psychrophila. FEMS Microbiol Lett. (1997) 151:191–196.
  • AGARWAL AK, ROGERS PD, BAERSON SR et al.: Genome-wide expression profiling of the response to polyene, pyrimidine, azole, and echinocandin antifungal agents inSaccharomyces cerevisiae. .1 Biol. Chem. (2003) 278:34998–35015.
  • GOES SG, MARTIN J: HSP90 chaperonecomplexes are required for the activity and stability of yeast protein kinases Miki Wee], and Swel. Eur. Biochein. (2001) 268:2281–2289.
  • JOHNSON KS, WELLS K, BOCK JV, NENE V, TAYLOR DW, CORDINGLEY JS: The 86-kilodalton antigen from Schistosoina mansoni is aheat-shock protein homologous to yeast HSP-90. Mol. Biochein. Paresitol (1989) 36:19–28.
  • ARIF AA, GAO L, DAVIS CD, HELM DS: Antibody response to heat shock proteins and histopathology in mice infected with Trypanosome cmzi and maintained at elevated temperature.Parasitol (1999) 85:1089–1099.
  • ROJAS PA, MARTIN V, NIGRO M et al: Expression of a cDNA encoding a Toxoplasina gondii protein belonging to the heat-shock 90 family and analysis of its antigenicity. FEMS Microbiol Lett. (2000) 190:209–213.
  • MARTINEZ J, PEREZ-SERRANO J, BERNADINA WE, RODRIGUEZ-CAABEIRO F: HSP60, HSP70 and HSP90 from Trichinella spiralis as targets of humoral immune response in rats. Parasitol Res. (2001) 87:453–458.
  • WIESGIGL M, CLOS J: The heat shock protein 90 of Leishinania donovani Med. Microbiol Iminunol Merl]. (2001) 190:27–31.
  • BANUMATHY G, SINGH V, PAVITHRA SR, TATU U: Heat shock protein 90 function is essential for Plasmodium falciparum growth in human erythrocytes. J. Biol. Chem. (2003) 278:18336–18345.
  • BONNEFOY S, ATTAL G, LANGSLEY G, TEKAIA F, MERCEREAU-PUIJALON 0: Molecular characterization of the heat shock protein 90 gene of the human malaria parasite Plasmodium falcipamm. MM. Biochem. Paresitol (1994) 67:157–170.
  • •The establishment of HSP90 as a target for immunotherapy in malaria.
  • ZHANG M, HISAEDA H, KANO S et al: Antibodies specific for heat shock proteins in human and murine malaria.Microbes Infect. (2001) 3:363–367.
  • BARD WELL JC, CRAIG EA: Eukaryotic Mr 83,000 heat shock protein has a homologue in Escherichia coli Proc. Nat] Acad. Sci. USA (1987) 84:5177–5181.
  • SPENCE J, GEORGOPOULOS C: Purification and properties of the Escherichia cob heat shock protein, HtpG. Biol. Chem. (1989) 264:4398–4403.
  • SPENCE J, CEGIELSKA A, GEORGOPOULOS C: Role of Escherichia cob heat shock proteins DnaK and HtpG (C62.5) in response tonutritional deprivation. .j Bacteria (1990) 172:7157–7166.
  • THOMAS JG, BANEY F: ClpB and HtpG facilitate de novo protein folding in stressed Escherichia colt cells. Ma Microbia (2000) 36:1360–1370.
  • HOMUTH G, DOMM S, KLEINER D, SCHUMANN W: Transcriptional analysis of major heat shock genes ofHelicobacter pylori J. Bacteria (2000) 182:4257–4263.
  • CLARK I, BURNIE JP, COKE AP, MATTHEWS RC, OPPENHEIM BA: Characterization of the antibody response in Corynebacteriumjeikeium septicaemias. Epidemia Infect. (1990) 105:229–236.
  • MATTHEWS RC: HSP 90, yeasts and Corynebacteriumjeikeium. Epidemia Infect. (1991) 107:273–283.
  • LOPATIN DE, COMBS A, SWEIER DG, FENNO JC, DHAMIJA S: Characterization of heat-inducible expression and cloning of HtpG (Hsp90 homologue) of Porphyromonas gingivalis. Infect. Inman. (2000) 68:1980–1987.
  • SHASTRY S JOYNER MJ: Geldanamycin attenuates NO-mediated dilation in human skin. Am. I Physia Heart Circ. Physia (2002) 282:232–236.
  • GARCIA-CARDENA G, FAN R, SHAH V et al: Dynamic activation of endothelial nitric oxide synthase by Hsp90. Nature (1998) 392:821–824.
  • •Study suggesting that human HSP90 might be involved in cardiovascular disease.
  • MONCADA S, PALMER RIVI, HIGGS EA: Nitric oxide: physiology, pathophysiology, and pharmacology. Pharmaca Rev (1991) 43:109–142.
  • COOKE JP, LOSORDO DW: Nitric oxideand angiogenesis. Circulation (2002) 105:2133–2135.
  • JOSEPH K THOLANIKUNNEL BG, KAPLAN AP: Heat shock protein 90 catalyzes activation of the prekallikrein-kininogen complex in the absence of Factor XII. Proc. Natl. Acad. Sci. USA (2002) 99:896–900.
  • JOSEPH K, THOLANIKUNNEL BG, KAPLAN AP: Activation of the bradykinin-forming cascade on endothelial cells: a role for heat shock protein 90.Int. Immunopharmaca (2002) 2:1851–1859.
  • •Mechanism by which HSP90 might initiate septic shock.
  • SHARIAT-MADAR Z, MAHDI F, SCHMAIER AH: Assembly and activation of the plasma kallikrein/kinin system: a new interpretation. Int. Immunopharmaca (2002) 2:1841–1849.
  • MATTHEWS R, BURNIE JP, LEE W: The application of epitope mapping in the development of a new serological test for systemic candidosis. Immuna Methods (1991) 143:73–79.
  • AL-DUGHAYM AM, MATTHEWS RC, BURNIE JP: Epitope mapping human heat shock protein 90 with sera from infected patients. FEMS Immuna Med. Microbia (1994) 8:43–48.
  • BURNIE J, MATTHEWS R: The role of antibodies against hsp90 in the treatment of fungal infections. Drug News Perspect. (2003) 16:205–210.
  • MATSUMOTO S, TANAKA E, NEMOTO TK et al.: Interaction between the N-terminal and middle regions is essential for the in vivo function of HSP90 molecular chaperone. J. Biol. Chem. (2002) 277:34959–34966.
  • •Best overall model of HSP90 function, identifying the three domains and allocating their functions.
  • PIPER PW, PANARETOU B,MILLSON SH et al.: Yeast is selectively hypersensitised to heat shock protein 90 (Hsp90)-targeting drugs with heterologous expression of the human Hsp90beta, a property that can be exploited in screens for new Hsp90 chaperone inhibitors.Gene (2003) 302:165–170.
  • LOU VION JF, WARTH R, PICARD D: Two eukaryote-specific regions of Hsp82 are dispensable for its viability and signal transduction functions in yeast. Proc. Natl. Acad. Sci. USA (1996) 93:13937–13942.
  • SCHEUFLER C, BRINKER A, BOURENKOV G et al.: Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp7O-Hsp90 multichaperone machine. Cell (2000) 101:199–210.
  • LOTZ GP, UN H, HARST A, OBERMANN WM: Ahal binds to the middle domain of Hsp90, contributes to client protein activation, and stimulates the ATPase activity of the molecular chaperone. J. Biol. Chem. (2003) 278:17228–17235.
  • WEGELE H, MUSCHLER P, BUNCK M, REINSTEIN J, BUCHNER J: Dissection of the contribution of individual domains to the ATPase mechanism of HSP90../. Biol. Chem. (2003) 278(41):39303–39310.
  • DUTTA R, INOUYE M: GHKL, an emergent ATPase/kinase super family. Trends Biochem. Sci. (2000) 25:24–28.
  • MEYER P, PRODROMOU C, HUB et al:Structural and functional analysis of the middle segment of hsp90: implications for ATP hydrolysis and client protein and co chaperone interactions. MM. Cell (2003) 11:647–658.
  • SOTI C, RACZ A, CSERMELY P:A nucleotide-dependent molecular switch controls ATP binding at the C-terminal domain of Hsp90. N-terminal nucleotide binding unmasks a C-terminal binding pocket. J Biol. Chem. (2002) 277:7066–7075.
  • •Demonstration that the middle domain of HSP90 is key to function.
  • NEUBERGER MS: Novartis Medal Lecture. Antibodies: a paradigm for the evolution of molecular recognition. Biochem. Soc. Trans. (2002) 30:341–350.
  • ROARK JH, BUSSEL JB, CINES DB, SIEGEL DL: Genetic analysis of auto antibodies in idiopathic thrombocytopenic purpura reveals evidence of clonal expansion and somatic mutation. Blood (2002) 100:1388–1398.
  • NZULA S, GOING JJ, STOTT DI: Antigen-driven clonal proliferation, somatic hyper mutation, and selection of B lymphocytes infiltrating human ductal breast carcinomas. Cancer Res. (2003) 63:3275–3280.
  • ZHOU J, LOTTENBACH KR, BARENKAMP SJ, LUCAS AH, REASON DC: Recurrent variable region gene usage and somatic mutation in the human antibody response to the capsular polysaccharide of Streptococcus pneumoniae type 23F. Infect. Immun. (2002) 70:4083–4091.
  • OHLIN M, ZOUALI M: The human antibody repertoire to infectious agents: implications for disease pathogenesis. MM. Immuna (2003) 40:1–11.
  • CHEN L, WILLIAMS BR, YANG CY et al.: Polyclonal Fab phage display libraries with a high percentage of diverse clones to Cryptosporidium parvum glycoproteins. Int. .1. Parasita (2003) 33:281–291.
  • MATTHEWS RC, BURNIE JP,HOWAT D, ROWLAND T, WALTON F: Autoantibody to heat-shock protein 90 can mediate protection against systemic candidosis. Immunology (1991) 74:20–24.
  • MATTHEWS R, HODGETTS S, BURNIE J: Preliminary assessment of a human recombinant antibody fragment to hsp90 in murine invasive candidiasis.Infect. Dis. (1995) 171:1668–1671.
  • TAVARES D, FERREIRA P,ARALA-CHAVES M: Increased resistance in BALB/c mice to reinfection with Candida albicansis due to immunoneutralization of a virulence-associated immunomodulatory protein. Microbiology (2003) 149:333–339.
  • HAN Y, KOZEL TR, ZHANG MX, MACGILL RS, CARROLL MC, CUTLER JE: Complement is essential for protection by an IgM and an IgG3 monoclonal antibody against experimental, hematogenously disseminated candidiasis.Immunol (2001) 167:1550–1557.
  • MIZUTANI S, ENDO M, INO-UE T et al.: Immunization with theCandida albicans membrane fraction and in combination with fluconazole protects against systemic fungal infections. Antimicrob. Agents Chemother. (2000) 44:243–247.
  • BURNIE JP, MATTHEWS RC: Heat shock protein 88 and Aspergillus infection. Clin. Microbiol (1991) 29:2099–2106.
  • SANTHANAM J, BURNIE JP: A PCR-based approach to sequence the Candida tropicalisHSP90 gene. FEMS Immunol Med. Microbiol (2000) 29:35–38.
  • EROLES P, SENTANDREU M,ELORZA MV, SENTANDREU R: The highly immunogenic enolase and Hsp7Op are adventitious Candida albicans cell wall proteins. Microbiology (1997) 143:313–320.
  • BROMURO C, LA VALLE R, SANDINI S et al.: A 70-kilodalton recombinant heat shock protein of Candida albicansis highly immunogenic and enhances systemic murine candidiasis. Infect. Inman. (1998) 66:2154–2162.
  • MATTHEWS R, WELLS C, BURNIE JP: Characterisation and cellular localisation of the immunodominant 47-Kda antigen of Candida albicans. .1 Med. Microbiol (1988) 27:227–232.
  • URBAN C, SOHN K, LOTTSPEICH F, BRUNNER H, RUPP S: Identification of cell surface determinants inCandida albicansreveals Tsalp, a protein differentially localized in the cell. FEBS Lett. (2003) 544:228–235.
  • CHILLER T, FARROKHSHAD K, BRUMMER E, STEVENS DA: Influence of human sera on the in vitro activity of the echinocandin caspofungin (MK-0991) against Aspergillus fumigatus. Antimicrob. Agents Chemother. (2000) 44:3302–3305.
  • FAIDAH HS, RIGG GP,MATTHEWS RC, BURNIE JP: Mycograb® and Amphotericin B resistant yeasts. American Socie0, for Microbiology (2003).
  • •Demonstration of Mycograbactivity against amphotericin B-resistant yeast isolates.
  • SREEDHAR AS, MIHALY K, PATO B et al.: Hsp90 inhibition accelerates cell lysis: anti-Hsp90 ribozyme reveals a complex mechanism of Hsp90 inhibitors involving both superoxide-and Hsp90-dependent events.' Biol. Chem. (2003) 278:35231–35240.
  • MURRAY HW, BROOKS EB, DEVECCHIO JL, HEINZEL FP: Immunoenhancement combined with amphotericin B as treatment for experimental visceral leishmaniasis. Antimicrob. Agents Chemother: (2003) 47:2513–2517.
  • BURNIE JP, ILLIDGE C, GREGORY C et al.: Mycograb®: preliminary clinical data. 41st ICAAC American Society for Microbiology (2001) .
  • MATTHEWS RC, BURNIE JP: A natural partner in combinatorial antifungal therapy. Vaccine (2003) (In Press).
  • •First clinical data on Mycograb.
  • BERGMAN A, SIEGAL ML: Evolutionarycapacitance as a general feature of complex gene networks. Nature (2003) 424:549–552.
  • •Fascinating discussion of the overall role of HSP90 in evolution.
  • STEARNS SC: Theoretical biology: safeguards and spurs. Nature (2003) 424:501–504.
  • WIEDERHOLD NP, LEWIS RE: The echinocandin antifungals: an overview of the pharmacology, spectrum and clinical efficacy. Expert Opin. Investig. Drugs (2003) 12:1313–1333.
  • MORA-DUARTE J, BETTS R, ROTSTEIN C et al.: Comparison of caspofungin and amphotericin B for invasive candidiasis. N Engl. I Med. (2002) 347:2020–2029.
  • http://www.neutecpharma.com NeuTec Pharma website.Affiliation

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.