Production of species-specific murine monoclonal antibodies against Cryptococcus neoformans which recognize a noncapsular exoantigen

Hamilton, Andrew J.; Bartholomew, M.A.; Figueroa, Jose I.; Fenelon, Lynda; Hay, Roderick J.

doi:10.1128/jcm.29.5.980-984.1991

Cited by 14 publications

(16 citation statements)

References 15 publications

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“…In contrast, few studies have investigated the antibody response to protein antigens. Hamilton and colleagues have generated murine monoclonal antibodies to glycoprotein antigens of 36 to 38 kDa and of 30 kDa and studied the human and rodent response to these antigens (19,21,39). These authors also analyzed the antibody response to cryptococcal proteins in human immunodeficiency virus (HIV)-infected patients with cryptococcosis by isoelectric focusing and concluded that there may be several immunodominant antigens (20).…”

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confidence: 99%

Antibody Response to Cryptococcus neoformans Proteins in Rodents and Humans

Chen¹,

Goldman

Doering

et al. 1999

Infect Immun

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The prevalence and specificity of serum antibodies toCryptococcus neoformans proteins was studied in mice and rats with experimental infection, in individuals with or without a history of potential laboratory exposure to C. neoformans, human immunodeficiency virus (HIV)-positive individuals who developed cryptococcosis, in matched samples from HIV-positive individuals who did not develop cryptococcosis, and in HIV-negative individuals. Rodents had little or no serum antibody reactive with C. neoformans proteins prior to infection. The intensity and specificity of the rodent antibody response were dependent on the species, the mouse strain, and the viability of the inoculum. All humans had serum antibodies reactive with C. neoformans proteins regardless of the potential exposure, the HIV infection status, or the subsequent development of cryptococcosis. Our results indicate (i) a high prevalence of antibodies reactive with C. neoformansproteins in the sera of rodents after cryptococcal infection and in humans with or without HIV infection; (ii) qualitative and quantitative differences in the antibody profiles of HIV-positive individuals; and (iii) similarities and differences between humans, mice, and rats with respect to the specificity of the antibodies reactive with C. neoformans proteins. The results are consistent with the view that C. neoformans infections are common in human populations, and the results have implications for the development of vaccination strategies against cryptococcosis.

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confidence: 99%

Antibody Response to Cryptococcus neoformans Proteins in Rodents and Humans

Chen¹,

Goldman

Doering

et al. 1999

Infect Immun

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“…Antibodies directed at secreted proteins with similar molecular masses have been described in the literature. For example, Hamilton and coworkers (8)(9)(10) have reported on antibodies that recognized 115-and 65-kDa antigens. Chen et al (3) have described numerous extracellular proteins that were immunogenic, and antibodies were identified to 75-and 30-kDa proteins secreted from one of the strains they studied.…”

Section: Discussionmentioning

confidence: 99%

An Opsonizing Monoclonal Antibody That Recognizes a Noncapsular Epitope Expressed on Cryptococcus neoformans

Merkel

Scofield

1999

Infect Immun

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A mouse hybridoma secreting a monoclonal antibody (MAb) that bound a noncapsular epitope expressed on C. neoformans was developed by immunizing BALB/c mice with formalin-killed serotype A yeasts. The hybridoma, designated CSFi, secreted an immunoglobulin G2b MAb that reacted with all C. neoformans serotypes tested, including the acapsular mutant ATCC 52817 (Cap67). Postsectioned immune electron microscopy revealed extensive binding of the MAb to the cell walls of both encapsulated and acapsular yeasts. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis and Western blot analysis of secreted antigens recovered from concentrated culture supernatants from both encapsulated and acapsular strains was conducted. The results showed that this MAb bound predominantly to antigens with molecular masses of approximately 75 and 100 kDa. A competitive enzyme-linked immunosorbent assay was used to demonstrate that the MAb was not cross-reactive with purified glucuronoxylomannan derived from either serotypes A or D. Experiments conducted with mouse peritoneal phagocytes and the mouse phagocyte-like cell line, J774A.1, demonstrated that the CSFi MAb opsonized the yeasts and increased their adherence to both types of phagocytic cells. We conclude, therefore, that antibodies directed at noncapsular epitopes can serve as opsonins and may have a role in modulating cryptococcal infection.

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“…Protein contents of samples were determined by the method of Lowry et al (14). SDSpolyacrylamide gel electrophoresis was carried out as previously described (8,9), using a 10% resolving gel. Gels were stained with silver stain (Bio-Rad, Hemel Hempstead, United Kingdom) to detect the presence of proteins.…”

Section: Influence Of Enzyme Treatment Of Fibronectin and Laminin On mentioning

confidence: 99%

“…Gels were stained with silver stain (Bio-Rad, Hemel Hempstead, United Kingdom) to detect the presence of proteins. Electrophoretic transfer of proteins from polyacrylamide gels to Immobilon-P membranes was carried out as previously described (8,9). Blotted proteins were assayed for fibronectin and laminin binding by first blocking overnight with 3% BSA in PBS buffer and then incubating for 6 h with agitation in PBS containing human fibronectin and murine laminin (each at 250 g/ml).…”

Section: Influence Of Enzyme Treatment Of Fibronectin and Laminin On mentioning

confidence: 99%

Recognition of Fibronectin by Penicillium marneffei Conidia via a Sialic Acid-Dependent Process and Its Relationship to the Interaction Between Conidia and Laminin

et al. 1999

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Adhesion of Penicillium marneffei conidia to the extracellular matrix protein laminin via a sialic acid-dependent process has previously been demonstrated. This study describes the interaction of P. marneffei conidia with fibronectin and examines the relationship of this process to the recognition of laminin via conidia. Immunofluorescence microscopy demonstrated that fibronectin bound to the surface of conidia and to phialides, but not to hyphae, in a pattern similar to that reported for laminin. Conidia were able to bind to fibronectin immobilized on microtiter plates in a concentration-dependent manner. However, binding to fibronectin (at any given concentration of protein and conidia) was less than that to laminin under equivalent conditions. Soluble fibronectin and antifibronectin antibody inhibited adherence of conidia to fibronectin in the plate adherence assay; soluble laminin also caused pronounced inhibition. Various monosaccharides and several peptides had no effect on adherence to fibronectin. However, N-acetylneuraminic acid abolished adherence to fibronectin, indicating that the interaction was mediated through a sialic acid-dependent process; the latter parallels observations of laminin binding by conidia. Fibronectin binding (and binding of laminin) was considerably reduced by prolonged preincubation of conidia with chymotrypsin, suggesting the protein nature of the binding site. Conidia from older cultures were more adherent to both immobilized fibronectin and laminin than conidia from younger cultures. Ligand affinity binding demonstrated the presence of a 20-kDa protein with the ability to bind both fibronectin and laminin. There would therefore appear to be a common receptor for the binding of fibronectin and laminin on the surface of P. marneffei, and the interaction described here maybe important in mediating attachment of the fungus to host tissue.

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Production of species-specific murine monoclonal antibodies against Cryptococcus neoformans which recognize a noncapsular exoantigen

Cited by 14 publications

References 15 publications

Antibody Response to Cryptococcus neoformans Proteins in Rodents and Humans

Antibody Response to Cryptococcus neoformans Proteins in Rodents and Humans

An Opsonizing Monoclonal Antibody That Recognizes a Noncapsular Epitope Expressed on Cryptococcus neoformans

Recognition of Fibronectin by Penicillium marneffei Conidia via a Sialic Acid-Dependent Process and Its Relationship to the Interaction Between Conidia and Laminin

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