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Titolo:
Structural identification of a key protective B-cell epitope in lyme disease antigen OspA
Autore:
Ding, W; Huang, XL; Yang, XH; Dunn, JJ; Luft, BJ; Koide, S; Lawson, CL;
Indirizzi:
Univ Rochester, Med Ctr, Dept Biochem & Biophys, Rochester, NY 14642 USA Univ Rochester Rochester NY USA 14642 & Biophys, Rochester, NY 14642 USA Brookhaven Natl Lab, Dept Biol, Upton, NY 11973 USA Brookhaven Natl Lab Upton NY USA 11973 ab, Dept Biol, Upton, NY 11973 USA SUNY Stony Brook, Dept Phys, Stony Brook, NY 11794 USA SUNY Stony Brook Stony Brook NY USA 11794 Phys, Stony Brook, NY 11794 USA SUNY Stony Brook, Sch Med, Div Infect Dis, Stony Brook, NY 11794 USA SUNY Stony Brook Stony Brook NY USA 11794 Dis, Stony Brook, NY 11794 USA Rutgers State Univ, Dept Chem, Piscataway, NJ 08854 USA Rutgers State Univ Piscataway NJ USA 08854 Chem, Piscataway, NJ 08854 USA
Titolo Testata:
JOURNAL OF MOLECULAR BIOLOGY
fascicolo: 5, volume: 302, anno: 2000,
pagine: 1153 - 1164
SICI:
0022-2836(20001006)302:5<1153:SIOAKP>2.0.ZU;2-G
Fonte:
ISI
Lingua:
ENG
Soggetto:
OUTER-SURFACE-PROTEIN; BORRELIA-BURGDORFERI OSPA; LAYER BETA-SHEET; ANTIBODY-BINDING DOMAINS; CRYSTAL-STRUCTURE; MOLECULAR REPLACEMENT; MONOCLONAL-ANTIBODIES; FAB FRAGMENT; CLASS-II; A OSPA;
Keywords:
lyme disease; outer surface protein A; X-ray diffraction; NMR spectroscopy; B-cell epitope;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
67
Recensione:
Indirizzi per estratti:
Indirizzo: Koide, S Univ Rochester, Med Ctr, Dept Biochem & Biophys, Rochester, NY 14642 USA Univ Rochester Rochester NY USA 14642 s, Rochester, NY 14642 USA
Citazione:
W. Ding et al., "Structural identification of a key protective B-cell epitope in lyme disease antigen OspA", J MOL BIOL, 302(5), 2000, pp. 1153-1164

Abstract

Outer surface protein A (OspA) is a major lipoprotein of the Borrelia burgorferi spirochete, the causative agent of Lyme disease. Vaccination with OspA generates an immune response that can prevent bacterial transmission to a mammalian host during the attachment of an infected tick. However, the protective capacity of immune sera cannot be predicted by measuring total anti-OspA antibody. The murine monoclonal antibody LA-2 defines an important protective B-cell epitope of OspA against which protective sera have strong levels of reactivity. We have now mapped the LA-2 epitope of OspA using both NMR chemical-shift perturbation measurements in solution and X-ray crystal structure determination. LA-2 recognizes the three surface-exposed loops of the C-terminal domain of OspA that are on the tip of the elongated molecule most distant from the lipid-modified N terminus. The structure suggeststhat the natural variation at OspA sequence position 208 in the first loopis a major limiting factor for antibody cross-reactivity between differentLyme disease-causing Borrelia strains. The unusual Fab-dominated lattice of the crystal also permits a rare view of antigen flexibility within an antigen:antibody complex. These results provide a rationale for improvements in OspA-based vaccines and suggest possible designs for more direct tests ofantibody protective levels in vaccinated individuals. (C) 2000 Academic Press.

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Documento generato il 29/11/20 alle ore 17:53:29