Access of antibody or trypsin to an integral outer membrane protein (P66) of Borrelia burgdorferi is hindered by Osp lipoproteins.
about
Borrelia recurrentis employs a novel multifunctional surface protein with anti-complement, anti-opsonic and invasive potential to escape innate immunitySpirochaetal lipoproteins and pathogenesisHuman pathogenic Borrelia spielmanii sp. nov. resists complement-mediated killing by direct binding of immune regulators factor H and factor H-like protein 1Borrelia burgdorferi and Treponema pallidum: a comparison of functional genomics, environmental adaptations, and pathogenic mechanismsConsensus computational network analysis for identifying candidate outer membrane proteins from Borrelia spirochetes.Structural modeling and physicochemical characterization provide evidence that P66 forms a β-barrel in the Borrelia burgdorferi outer membrane.A comprehensive approach to identification of surface-exposed, outer membrane-spanning proteins of Leptospira interrogans.Comparison of protection in rabbits against host-adapted and cultivated Borrelia burgdorferi following infection-derived immunity or immunization with outer membrane vesicles or outer surface protein A.Fibronectin-binding protein of Borrelia hermsii expressed in the blood of mice with relapsing fever.Development and validation of a FACS-based lipoprotein localization screen in the Lyme disease spirochete Borrelia burgdorferi.Analysis of antibody response to invariable regions of VlsE, the variable surface antigen of Borrelia burgdorferi.Protection elicited by native outer membrane protein Oms66 (p66) against host-adapted Borrelia burgdorferi: conformational nature of bactericidal epitopes.In vitro and in vivo neutralization of the relapsing fever agent Borrelia hermsii with serotype-specific immunoglobulin M antibodies.Recognition of multiple antibody epitopes throughout Borrelia burgdorferi p66, a candidate adhesin, in patients with early or late manifestations of Lyme disease.P13, an integral membrane protein of Borrelia burgdorferi, is C-terminally processed and contains surface-exposed domainsPurification and characterization of Borrelia burgdorferi from feeding nymphal ticks (Ixodes scapularis)Decorin-binding protein A (DbpA) of Borrelia burgdorferi is not protective when immunized mice are challenged via tick infestation and correlates with the lack of DbpA expression by B. burgdorferi in ticks.Borrelia burgdorferi RevA antigen is a surface-exposed outer membrane protein whose expression is regulated in response to environmental temperature and pHBmpA is a surface-exposed outer-membrane protein of Borrelia burgdorferiTargeted mutation of the outer membrane protein P66 disrupts attachment of the Lyme disease agent, Borrelia burgdorferi, to integrin alphavbeta3Simultaneous coexpression of Borrelia burgdorferi Erp proteins occurs through a specific, erp locus-directed regulatory mechanism.Variable VlsE is critical for host reinfection by the Lyme disease spirochete.Global analysis of Borrelia burgdorferi genes regulated by mammalian host-specific signalsProtective niche for Borrelia burgdorferi to evade humoral immunitySpecificity and role of the Borrelia burgdorferi CtpA protease in outer membrane protein processing.Characterization of multiprotein complexes of the Borrelia burgdorferi outer membrane vesicles.Determination of Borrelia surface lipoprotein anchor topology by surface proteolysis.Probing the Borrelia burgdorferi surface lipoprotein secretion pathway using a conditionally folding protein domainEvaluation of the Importance of VlsE Antigenic Variation for the Enzootic Cycle of Borrelia burgdorferiThe enolase of Borrelia burgdorferi is a plasminogen receptor released in outer membrane vesicles.Borrelia burgdorferi BBA74, a periplasmic protein associated with the outer membrane, lacks porin-like propertiesOuter membrane proteins of pathogenic spirochetes.Alp, an arthropod-associated outer membrane protein of Borrelia species that cause relapsing feverComprehensive Spatial Analysis of the Borrelia burgdorferi Lipoproteome Reveals a Compartmentalization Bias toward the Bacterial SurfaceGenetic basis for retention of a critical virulence plasmid of Borrelia burgdorferi.Cross-species surface display of functional spirochetal lipoproteins by recombinant Borrelia burgdorferi.Antigenic Variation in Bacterial Pathogens.A Borrelia burgdorferi Surface-Exposed Transmembrane Protein Lacking Detectable Immune Responses Supports Pathogen Persistence and Constitutes a Vaccine TargetFunctional Equivalence of OspA and OspB, but Not OspC, in Tick Colonization by Borrelia burgdorferiOuter surface protein A protects Lyme disease spirochetes from acquired host immunity in the tick vector.
P2860
Q21143848-03B06CF0-DF8B-4678-B08A-741DDEEE5E02Q24648165-6392100E-2C80-4A8D-9624-93067CD3A84CQ24672482-AE2FAF4D-8B26-479B-BE5D-0B73E96CC28FQ24672670-146003D6-0355-43D0-85B8-E4C85128DF12Q30152759-E0E09B81-5EF8-49C5-9A10-40A45153A563Q30153471-0F45456F-4B62-49B6-8E39-B677931B333AQ30157215-5CA1D0AE-71A6-4F24-B691-F3D11B7B822DQ33598183-D84C67E6-F4DD-45E1-AA2E-AD668575DC93Q33603094-5C5977D8-61F0-4B32-87B8-7D22ECAAF1E2Q33737127-59B89706-872C-45AD-A4CF-2F7342F11F3DQ34002894-0291A8F6-A909-47B1-B075-5DF52514D3F5Q34004241-CB6A0B98-4145-496E-B83F-63841B06B64AQ34006035-E03ED644-1A36-45E4-814F-56438EBDA2A8Q34006591-2B884D02-2C46-40BC-AFA1-991AE2DCA283Q34007376-84C3A816-2E64-4603-869D-29D15FCED301Q34007498-C8DBE73B-EA4A-47E9-BD4B-82C671D93750Q34007939-714ABEBA-5575-49A1-9C21-88032121936BQ34008806-A1D756E2-6C89-4CA6-9FC6-B9F3CD69E0BEQ34034838-6B5B03AF-4EC3-421E-8C20-68395034D6B0Q34197056-E286AC19-08E5-417C-B09F-C114A0C563EFQ34316819-0DDD8C03-6BAE-4AD6-B832-753D2F725A5DQ34674810-F96EC4B3-4810-467B-B566-C4BF390BAF9DQ35011172-9AE21FB7-1A56-4139-B59C-4328F536BF3DQ35103113-963E3335-66F9-41D9-B4AC-E884C659FAC3Q35272739-1779EC6F-B988-4D9C-98C8-DE8E2CA14E6FQ35291688-6E778AFE-D6DE-44A6-97F6-D3F4293655EBQ35530959-29B253FC-D844-4DFE-84A4-823E4E8398B3Q35598789-CD05A1DB-7EA5-4FD8-B064-8F400ECCC0A9Q35609906-2284E84A-7D04-4303-A8EE-27E481AC4AA6Q35665483-82BEC649-743E-4FAA-A264-830D253C0B54Q35759441-055F2835-83DF-4B0D-95E5-BBBC786C7BEDQ35902245-E972888F-1090-4C62-80DB-DCCE13D8C9A7Q35944087-BF7FDB81-6B41-42DD-B11C-BC7B33EC94ABQ36245018-14295D06-BBBB-44D5-A5D1-8CD538A996F6Q36434723-5A669C63-884F-4308-B29A-68430FA2A8E6Q36576612-102081FD-1223-4FC4-9E41-3449DE75B09FQ36725495-EDFCE50D-5C1A-4C3E-B4ED-CF2A51E214B5Q36871934-C126312B-6D8B-4A34-AB69-B923E5C533EAQ36888491-81B4F8D2-FDE1-4F13-B3D4-206E4C009F29Q36949994-1D65250B-B9F4-46A4-A7F7-B16955296166
P2860
Access of antibody or trypsin to an integral outer membrane protein (P66) of Borrelia burgdorferi is hindered by Osp lipoproteins.
description
1999 nî lūn-bûn
@nan
1999 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի հունիսին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Access of antibody or trypsin ...... hindered by Osp lipoproteins.
@ast
Access of antibody or trypsin ...... hindered by Osp lipoproteins.
@en
Access of antibody or trypsin to an integral outer membrane protein
@nl
type
label
Access of antibody or trypsin ...... hindered by Osp lipoproteins.
@ast
Access of antibody or trypsin ...... hindered by Osp lipoproteins.
@en
Access of antibody or trypsin to an integral outer membrane protein
@nl
prefLabel
Access of antibody or trypsin ...... hindered by Osp lipoproteins.
@ast
Access of antibody or trypsin ...... hindered by Osp lipoproteins.
@en
Access of antibody or trypsin to an integral outer membrane protein
@nl
P2860
P921
P1476
Access of antibody or trypsin ...... s hindered by Osp lipoproteins
@en
P2093
A G Barbour
P2860
P304
P407
P577
1999-06-01T00:00:00Z