Evidence map›Paper›PMID 11292763›Full record

ArticleInfection and immunity2001

Molecular basis for immunoglobulin M specificity to epitopes in Cryptococcus neoformans polysaccharide that elicit protective and nonprotective antibodies.

A Nakouzi, P Valadon, J Nosanchuk, N Green, A Casadevall

Open access · greenAbstract read
In one paragraph

Article in Infection and immunity, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.7field-weighted citation impact, top 10% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

12 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
  2. Frontiers in cellular and infection microbiology · 2022
    Review
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 4 institutions in 1 country.

A NakouziDivision of Infectious Diseases, Department of Medicine, Albert Einstein College of Medicine, Bronx, New York 10461, USA.
P Valadon
J Nosanchuk
N Green
A Casadevall
Albert Einstein College of Medicine · USOffice of Infectious Diseases · USPediatrics and Genetics · USSidney Kimmel Cancer Center · US

Funding

Synergy of Host Defense Mechanisms in the LungR01HL059842 · NHLBI · YESHIVA UNIVERSITY · PI CASADEVALL, ARTURO · 1997 to 2023
$7.4M
PROTECTIVE ANTIBODIES FOR CRYPTOCOCCAL INFECTIONSR01AI033774 · NIAID · YESHIVA UNIVERSITY · PI CASADEVALL, ARTURO · 1994 to 2014
$5.6M
MELANOGENESIS IN CRYPTOCOCCUS NEOFORMANSK08AI001489 · NIAID · YESHIVA UNIVERSITY · PI NOSANCHUK, JOSHUA D · 1998 to 2002
$378k
NHLBI NIH HHS HL-59842-01NHLBI NIH HHS R01 HL059842NIAID NIH HHS AI01489NIAID NIH HHS AI3342NIAID NIH HHS AI33774NIAID NIH HHS R01 AI033774
6 · The paper itself

Abstract

The protective efficacy of antibodies (Abs) to Cryptococcus neoformans glucuronoxylomannan (GXM) is dependent on Ab fine specificity. Two clonally related immunoglobulin M monoclonal Abs (MAbs) (12A1 and 13F1) differ in fine specificity and protective efficacy, presumably due to variable (V)-region sequence differences resulting from somatic mutations. MAb 12A1 is protective and produces annular immunofluorescence (IF) on serotype D C. neoformans, while MAb 13F1 is not protective and produces punctate IF. To determine the Ab molecular determinants responsible for the IF pattern, site-directed mutagenesis of the MAb 12A1 heavy-chain V region (V(H)) was followed by serological and functional studies of the various mutants. Changing two selected amino acids in the 12A1 V(H) binding cavity to the corresponding residues in the 13F1 V(H) altered the IF pattern from annular to punctate, reduced opsonic efficacy, and abolished recognition by an anti-idiotypic Ab. Analysis of the binding of the various mutants to peptide mimetics revealed that different amino acids were responsible for GXM binding and peptide specificity. The results suggest that V-region motifs associated with annular binding and opsonic activity may be predictive of Ab efficacy against C. neoformans. This has important implications for immunotherapy and vaccine design that are reinforced by the finding that GXM and peptide reactivities are determined by different amino acid residues.

Indexed as

Amino Acid SequenceAnimalsAntibodies, Anti-IdiotypicAntibodies, FungalAntibodies, MonoclonalAntibody SpecificityBinding Sites, AntibodyCell LineCryptococcus neoformansFluorescent Antibody TechniqueImmunoglobulin MMiceMolecular Sequence DataMutagenesis, Site-DirectedPhagocytosisPolysaccharidesAntibodies, Anti-IdiotypicAntibodies, FungalAntibodies, MonoclonalglucuronoxylomannanImmunoglobulin MPolysaccharides

Identifiers

PMID11292763
PMCPMC98299
OpenAlexW2113306402

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.