Crystal structure of outer surface protein A (OspA) ofBorrelia burgdorfericomplexed with a murine monoclonal Fab
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چکیده
منابع مشابه
Crystal structure of Neisserial surface protein A (NspA), a conserved outer membrane protein with vaccine potential.
The neisserial surface protein A (NspA) from Neisseria meningitidis is a promising vaccine candidate because it is highly conserved among meningococcal strains and induces bactericidal antibodies. NspA is a homolog of the Opa proteins, which mediate adhesion to host cells. Here, we present the crystal structure of NspA, determined to 2.55-A resolution. NspA forms an eight-stranded antiparallel ...
متن کاملSafety, immunogenicity, and efficacy of Borrelia burgdorferi outer surface protein A (OspA) vaccine: A meta-analysis.
INTRODUCTION Lyme borreliosis, caused by Borrelia burgdorferi sensu stricto in the United States and by several Borrelia species in Europe and Asia, has a great impact on the health of the global population. There are human vaccines available, such as the outer surface protein A (OspA) vaccine, but still more evidence is needed to verify its function. We investigated the safety, immunogenicity,...
متن کاملRelationship between immunity to Borrelia burgdorferi outer-surface protein A (OspA) and Lyme arthritis.
Antibiotic-refractory Lyme arthritis may result from Borrelia burgdorferi-induced autoimmunity in affected joints. Such patients usually have certain HLA-DRB1 molecules that bind an epitope of B. burgdorferi outer-surface protein A (OspA₁₆₃₋₁₇₅), and cellular and humoral immune responses to OspA are greater in patients with antibiotic-refractory arthritis than in those with antibiotic-responsiv...
متن کاملStructure of rotavirus outer-layer protein VP7 bound with a neutralizing Fab.
Rotavirus outer-layer protein VP7 is a principal target of protective antibodies. Removal of free calcium ions (Ca2+) dissociates VP7 trimers into monomers, releasing VP7 from the virion, and initiates penetration-inducing conformational changes in the other outer-layer protein, VP4. We report the crystal structure at 3.4 angstrom resolution of VP7 bound with the Fab fragment of a neutralizing ...
متن کاملThree-dimensional structure of Fab R19.9, a monoclonal murine antibody specific for the p-azobenzenearsonate group.
The crystal structure of Fab R19.9, derived from an anti-p-azobenzenearsonate monoclonal antibody, has been determined and refined to 2.8-A resolution by x-ray crystallographic techniques. Monoclonal antibody R19.9 (IgG2b kappa) shares some idiotopes with a major idiotype (CRIA) associated with A/J anti-p-azobenzenearsonate antibodies. The amino acid sequences of the variable (V) parts of the h...
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ژورنال
عنوان ژورنال: Acta Crystallographica Section A Foundations of Crystallography
سال: 1996
ISSN: 0108-7673
DOI: 10.1107/s0108767396090526