ArticleThe Journal of experimental medicine1991
The mouse antibody response to infection with Cryptococcus neoformans: VH and VL usage in polysaccharide binding antibodies.
Article in The Journal of experimental medicine, 1991. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.
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Who cites it
56 citing papers in PubMed, 118 citations in OpenAlex.
- Engineering affinity-matured variants of an anti-polysialic acid monoclonal antibody with superior cytotoxicity-mediating potency.Cell chemical biology · 2025Article
- New insights into antibody structure with implications for specificity, variable region restriction and isotype choice.Nature reviews. Immunology · 2025Review
- Synthetic Glycans Reveal Determinants of Antibody Functional Efficacy against a Fungal Pathogen.ACS infectious diseases · 2024Article
- Monoclonal Antibodies against Cell Wall Chitooligomers as Accessory Tools for the Control of Cryptococcosis.Antimicrobial agents and chemotherapy · 2021Article
- Identification of Disease-Associated Cryptococcal Proteins Reactive With Serum IgG From Cryptococcal Meningitis Patients.Frontiers in immunology · 2021Article
- Article
- Distinct and redundant roles of exonucleases in Cryptococcus neoformans: implications for virulence and mating.Fungal genetics and biology : FG & B · 2014Article
- Molecular characterization of the early B cell response to pulmonary Cryptococcus neoformans infection.Journal of immunology (Baltimore, Md. : 1950) · 2012Article
- Limiting CDR-H3 diversity abrogates the antibody response to the bacterial polysaccharide α 1→3 dextran.Journal of immunology (Baltimore, Md. : 1950) · 2011Article
- Antibodies raised against chlamydial lipopolysaccharide antigens reveal convergence in germline gene usage and differential epitope recognition.Biochemistry · 2010Article
- The common Cryptococcus neoformans glucuronoxylomannan M2 motif elicits non-protective antibodies.Vaccine · 2009Article
- Evidence for preferential Ig gene usage and differential TdT and exonuclease activities in human naïve and memory B cells.Molecular immunology · 2007Article
- Specific antibody can prevent fungal biofilm formation and this effect correlates with protective efficacy.Infection and immunity · 2005Article
- Molecular analysis of monoclonal antibodies to group variant capsular polysaccharide of Neisseria meningitidis: recurrent heavy chains and alternative light chain partners.Molecular immunology · 2005Article
- UGD1, encoding the Cryptococcus neoformans UDP-glucose dehydrogenase, is essential for growth at 37 degrees C and for capsule biosynthesis.Eukaryotic cell · 2004Article
- Cas3p belongs to a seven-member family of capsule structure designer proteins.Eukaryotic cell · 2004Article
- Antibodies produced in response to Cryptococcus neoformans pulmonary infection in mice have characteristics of nonprotective antibodies.Infection and immunity · 2004Article
- Antibody to Cryptococcus neoformans glucuronoxylomannan inhibits the release of capsular antigen.Infection and immunity · 2004Article
- Remarkably similar antigen receptors among a subset of patients with chronic lymphocytic leukemia.The Journal of clinical investigation · 2004Article
- Fcgamma receptor I- and III-mediated macrophage inflammatory protein 1alpha induction in primary human and murine microglia.Infection and immunity · 2002Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Cryptococcus neoformans is a ubiquitous fungus that can cause serious infections in humans. The fungus has a polysaccharide (C. neoformans capsular polysaccharide; CNPS) capsule that contributes to its pathogenicity and can elicit an antibody response. Nevertheless, only 4 of 60 BALB/c mice chronically infected with C. neoformans had a detectable increase in serum anti-CNPS. The sera of three responder mice contained both IgM and IgG anti-CNPS antibody, and the titers of lambda and kappa anti-CNPS antibody were approximately equal. Eight IgM and one IgG3 monoclonal antibodies (mAbs) were generated from the spleen of one responder mouse, and one IgA was generated from the spleen of another mouse. Seven of the IgMs, the IgG3, and the IgA mAb had lambda light chains and were specific for serotype D CNPS. Molecular analysis confirmed that this was a highly restricted antibody response. All of the D-specific antibodies used VH441, JH3, and either V lambda 2/J lambda 2 or V lambda 1/J lambda 1, and all had the same heavy chain CDR3 amino acid sequence, even though there were differences in the nucleotide sequence of the N/D segment. One IgM mAb reacted with both serotype A and D CNPS, and this mAb used different VH and JH genetic elements and had kappa light chains. All the anti-CNPS mAbs used J proximal VH gene elements that have previously been shown to bind dextran and other polysaccharides. Sequence and Southern blot analysis indicate that the serotype-D CNPS-specific mAbs arose from only a few precursor B cells.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.