Production of antibodies to antigens of Candida albicans in CBA/H mice

Costantino, Paul; Franklyn, Kathleen M.; Gare, Norman F.; Warmington, John R.

doi:10.1128/iai.62.4.1400-1405.1994

Cited by 20 publications

(15 citation statements)

References 20 publications

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“…HSP70s play an important immunologic role in a variety of infections, such as malaria (2), trypanosomiasis (16), bilharziasis (23), leishmaniasis (34), and diseases caused by chlamydiae (5,9,31,51) and mycobacteria (15,44). The involvement of HSP90 in fungal infections such as candidiasis has also been described (8), while HSP88 is involved in aspergillosis (6). Furthermore, a member of the HSP70 family of Histoplasma capsulatum was recognized as a target of cell-mediated, protective immunity (17).…”

Section: Discussionmentioning

confidence: 99%

A 77-kilodalton protein of Cryptococcus neoformans, a member of the heat shock protein 70 family, is a major antigen detected in the sera of mice with pulmonary cryptococcosis

et al. 1997

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Heat shock proteins (HSPs) from several pathogenic microbes have been shown to be target molecules of humoral responses as well as cellular immune responses. However, little is known about target molecules in pulmonary cryptococcosis. Western blotting analysis revealed that experimentally induced pulmonary cryptococcosis in (BALB/c ؋ DBA/2)F 1 mice was associated with the appearance of serum antibodies to a 77-kDa protein derived from Cryptococcus neoformans as well as to 18-, 22-, 25-, 36-, and 94-kDa proteins. Since the 77-kDa band also reacted with rabbit polyclonal antibodies against 70-kDa HSP (HSP70) family members, the protein was predicted to be a member of the HSP70 family. We also purified HSP70 directly from a C. neoformans cell extract by Mono Q fast protein liquid chromatography and ATP-agarose affinity column chromatography and showed that it was positive in immunoblot analysis using either serum from C. neoformans-infected mice or rabbit anti-HSP70 antibodies. N-terminal amino acid sequencing of this purified protein confirmed that the 77-kDa protein was a member of the HSP70 protein family. A 66-kDa protein, which coincidentally purified with the HSP70 protein and was identified as a member of the HSP60 family by N-terminal amino acid sequencing, was not reactive with sera from C. neoformans-infected mice. Thus, a protein associated with the HSP70 family and derived from C. neoformans was a major target molecule of the humoral response in murine pulmonary cryptococcosis.

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Section: Discussionmentioning

confidence: 99%

A 77-kilodalton protein of Cryptococcus neoformans, a member of the heat shock protein 70 family, is a major antigen detected in the sera of mice with pulmonary cryptococcosis

et al. 1997

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“…Most of the nonconservative substitutions were between amino acids 557-644, which was perceived as an area key to the antigenicity of the molecule (La Valle et al, 1995). Immunization with a recombinant of this molecule produced a murine antibody response against bands at 70 kDa, which were suggested as similar to a 75-kDa hsp shown previously as immunodominant in CBA/H mice during systemic candidiasis (Costantino et al, 1994). Immunoscreening a mycelial expression library further identified a sequence which was 99.3% identical to C. albicans HSP70 and approximately 79% identical to the sequences of SSA1-4 (Eroles et al, 1995).…”

Section: Hsp70mentioning

confidence: 91%

“…Other hsps have been identified by growing C. albicans at 42 1C. Induced bands on electrophoresis were visible at 28, 38, 47 and 60 kDa, although the predominant response was in the 70-110-kDa range (Franklyn & Warmington, 1994). Two-dimensional electrophoresis of extracts of C. albicans identified homologues of S. cerevisiae hsp90, Ssa1, Ssa4, Ssb1/Kar2, Ss31/ Pdr13 and hsp104 .…”

Section: Hsps and Pathogenic Fungi Candida Albicansmentioning

confidence: 99%

“…The second, an antigen of apparent mass 47 kDa, was identified as the carboxy fragment of C. albicans hsp90 (Cho et al, 2003). It was more abundant and could be distinguished from enolase by the pattern of cross-reactivity with an enolase-specific monoclonal antibody (Franklyn & Warmington, 1994). Debate on the molecular size of the parent molecule has been centred on a predicted molecule mass of 81 kDa (Bromuro et al, 1998;Sandini et al, 2002).…”

Section: Hsp90 and Antibodies In Fungal Infectionmentioning

confidence: 99%

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Fungal heat-shock proteins in human disease

Burnie¹,

Carter²,

Hodgetts³

et al. 2006

FEMS Microbiol Rev

135

108

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Heat-shock proteins (hsps) have been identified as molecular chaperones conserved between microbes and man and grouped by their molecular mass and high degree of amino acid homology. This article reviews the major hsps of Saccharomyces cerevisiae, their interactions with trehalose, the effect of fermentation and the role of the heat-shock factor. Information derived from this model, as well as from Neurospora crassa and Achlya ambisexualis, helps in understanding the importance of hsps in the pathogenic fungi, Candida albicans, Cryptococcus neoformans, Aspergillus spp., Histoplasma capsulatum, Paracoccidioides brasiliensis, Trichophyton rubrum, Phycomyces blakesleeanus, Fusarium oxysporum, Coccidioides immitis and Pneumocystis jiroveci. This has been matched with proteomic and genomic information examining hsp expression in response to noxious stimuli. Fungal hsp90 has been identified as a target for immunotherapy by a genetically recombinant antibody. The concept of combining this antibody fragment with an antifungal drug for treating life-threatening fungal infection and the potential interactions with human and microbial hsp90 and nitric oxide is discussed.

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“…hsp70 is also recognized by sera of patients with oral and esophageal infection (524). It has also been demonstrated that the antibody response in a murine model of systemic candidiasis includes reactivity against a 75-kDa hsp (85). Due to the high levels of homology between the different hsp70s, a combination of antibodies to the different members of this family in C. albicans as well as to hsp70s from other microorganisms may be present in the host serum.…”

Section: Heat Shock Proteinsmentioning

confidence: 99%

Cell Wall and Secreted Proteins ofCandida albicans: Identification, Function, and Expression

Chaffin

López-Ribot

Casanova

et al. 1998

Microbiol Mol Biol Rev

666

344

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SUMMARY The cell wall is essential to nearly every aspect of the biology and pathogenicity of Candida albicans. Although it was intially considered an almost inert cellular structure that protected the protoplast against osmotic offense, more recent studies have demonstrated that it is a dynamic organelle. The major components of the cell wall are glucan and chitin, which are associated with structural rigidity, and mannoproteins. The protein component, including both mannoprotein and nonmannoproteins, comprises some 40 or more moieties. Wall proteins may differ in their expression, secretion, or topological location within the wall structure. Proteins may be modified by glycosylation (primarily addition of mannose residues), phosphorylation, and ubiquitination. Among the secreted enzymes are those that are postulated to have substrates within the cell wall and those that find substrates in the extracellular environment. Cell wall proteins have been implicated in adhesion to host tissues and ligands. Fibrinogen, complement fragments, and several extracellular matrix components are among the host proteins bound by cell wall proteins. Proteins related to the hsp70 and hsp90 families of conserved stress proteins and some glycolytic enzyme proteins are also found in the cell wall, apparently as bona fide components. In addition, the expression of some proteins is associated with the morphological growth form of the fungus and may play a role in morphogenesis. Finally, surface mannoproteins are strong immunogens that trigger and modulate the host immune response during candidiasis.

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Production of antibodies to antigens of Candida albicans in CBA/H mice

Abstract: Reported targets of the specific immune responses to Candida albicans in human candidiasis include a 47-kDa breakdown product of a 90-kDa heat shock protein (HSP 90) (R.

Cited by 20 publications

References 20 publications

A 77-kilodalton protein of Cryptococcus neoformans, a member of the heat shock protein 70 family, is a major antigen detected in the sera of mice with pulmonary cryptococcosis

A 77-kilodalton protein of Cryptococcus neoformans, a member of the heat shock protein 70 family, is a major antigen detected in the sera of mice with pulmonary cryptococcosis

Fungal heat-shock proteins in human disease

Cell Wall and Secreted Proteins ofCandida albicans: Identification, Function, and Expression

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