Linked Life Data

8760499

Source:http://linkedlifedata.com/resource/pubmed/id/8760499

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1996-9-17
pubmed:abstractText
Cryptococcus neoformans is an encapsulated fungus that causes a life-threatening meningoencephalitis in patients with AIDS. Monoclonal antibodies to the capsular glucuronoxylomannan can modulate the infection in mice, but the epitopes on this complex polysaccharide recognized by protective and non-protective antibodies have not been defined. We have used 2H1, one of our most protective antibodies, to screen phage display peptide libraries for peptide mimotopes that would allow us to explore the fine specificity of anti-cryptococcal polysaccharide antibodies. Hexa- and decapeptides have been identified with sequence homologies that define four motifs: 1, (E)TPXWM/LM/L; 2, W/YXWM/ LYE; 3, DWXDW; and 4, (Ar)WDGQ(Ar). Peptides representing these motifs compete with each other for a shared binding site that overlaps the polysaccharide binding site. Motifs 1 and 2 confer high affinity binding, and PA1, which displays a motif 1 peptide with the sequence LQYTPSWMLV, binds to 2H1 with a Kd of 295 nM. Analysis of the interaction between the 2H1 binding peptides and 24 structurally related anti-polysaccharide antibodies reveals a complex pattern of reactivity that strongly suggests binding to or close to the complementary determining regions. Furthermore, those antibodies that have been shown to have different specificity, and in some cases different protective potential, do not bind any of the peptides selected by the protective 2H1 antibody. This study shows that peptide mimotopes for a complex microbial polysaccharide can be identified by screening phage peptide libraries and demonstrates the usefulness of such peptides in analyzing closely related interactive sites of proteins in general and of antibodies in particular.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0022-2836
pubmed:author
pubmed:issnType
Print
pubmed:day
9
pubmed:volume
261
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
11-22
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed-meshheading:8760499-Amino Acid Sequence, pubmed-meshheading:8760499-Animals, pubmed-meshheading:8760499-Antibodies, Fungal, pubmed-meshheading:8760499-Antibodies, Monoclonal, pubmed-meshheading:8760499-Antibody Specificity, pubmed-meshheading:8760499-Bacteriophages, pubmed-meshheading:8760499-Base Sequence, pubmed-meshheading:8760499-Binding, Competitive, pubmed-meshheading:8760499-Binding Sites, Antibody, pubmed-meshheading:8760499-Cryptococcus neoformans, pubmed-meshheading:8760499-DNA Probes, pubmed-meshheading:8760499-Enzyme-Linked Immunosorbent Assay, pubmed-meshheading:8760499-Epitopes, pubmed-meshheading:8760499-Gene Library, pubmed-meshheading:8760499-Immunoglobulin Fab Fragments, pubmed-meshheading:8760499-Mice, pubmed-meshheading:8760499-Mice, Inbred BALB C, pubmed-meshheading:8760499-Molecular Sequence Data, pubmed-meshheading:8760499-Oligopeptides, pubmed-meshheading:8760499-Polysaccharides, pubmed-meshheading:8760499-Sequence Analysis
pubmed:year
1996
pubmed:articleTitle
Peptide libraries define the fine specificity of anti-polysaccharide antibodies to Cryptococcus neoformans.
pubmed:affiliation
Department of Cell Biology, Albert Einstein College of Medicine, Bronx, NY 10461, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't