The crystal structures of EAP domains from Staphylococcus aureus reveal an unexpected homology to bacterial superantigens.
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Staphylococcal manipulation of host immune responsesStaphylococcus aureus secretes a unique class of neutrophil serine protease inhibitorsStuck in the Middle: Fibronectin-Binding Proteins in Gram-Positive BacteriaSurfactant protein A (SP-A)-mediated clearance of Staphylococcus aureus involves binding of SP-A to the staphylococcal adhesin eap and the macrophage receptors SP-A receptor 210 and scavenger receptor class AStaphylococcus aureus extracellular adherence protein triggers TNFα release, promoting attachment to endothelial cells via protein A.Complement evasion by human pathogens.Expression, purification, and characterization of protective MPT64 antigen protein and identification of its multimers isolated from nontoxic Mycobacterium tuberculosis H37Ra.The extracellular adherence protein from Staphylococcus aureus inhibits the classical and lectin pathways of complement by blocking formation of the C3 proconvertaseCharacterization of the fibrinogen binding domain of bacteriophage lysin from Streptococcus mitis.Suppression of experimental autoimmune encephalomyelitis by extracellular adherence protein of Staphylococcus aureus.STRALCP--structure alignment-based clustering of proteins.Crystallization and X-ray diffraction analysis of the complement component-3 (C3) inhibitory domain of Efb from Staphylococcus aureus.The Staphylococcus aureus extracellular adherence protein (Eap) adopts an elongated but structured conformation in solution.The Staphyloccous aureus Eap protein activates expression of proinflammatory cytokines.Structure and flexibility within proteins as identified through small angle X-ray scatteringRepeating structures of the major staphylococcal autolysin are essential for the interaction with human thrombospondin 1 and vitronectin.Functional, biochemical and 3D studies of Mycobacterium tuberculosis protein peptides for an effective anti-tuberculosis vaccine.Mapping the transcription start points of the Staphylococcus aureus eap, emp, and vwb promoters reveals a conserved octanucleotide sequence that is essential for expression of these genes.Novel Evasion Mechanisms of the Classical Complement Pathway.Staphylococcus aureus Aggregation and Coagulation Mechanisms, and Their Function in Host-Pathogen Interactions.Staphylococcus aureus Manipulates Innate Immunity through Own and Host-Expressed Proteases(1)H, (15)N, and (13)C resonance assignments of Staphylococcus aureus extracellular adherence protein domain 4Staphylococcus aureus protects its immune-evasion proteins against degradation by neutrophil serine proteases.Expression, purification and crystallization of Streptococcus dysgalactiae-derived mitogen.Use of peptide-major histocompatibility complex tetramer technology to study interactions between Staphylococcus aureus proteins and human cells.eap Gene as novel target for specific identification of Staphylococcus aureus.More than one tandem repeat domain of the extracellular adherence protein of Staphylococcus aureus is required for aggregation, adherence, and host cell invasion but not for leukocyte activation.Evidence for multiple modes of neutrophil serine protease recognition by the EAP family of Staphylococcal innate immune evasion proteins.1H, 15N, and 13C resonance assignments of the third domain from the S. aureus innate immune evasion protein Eap.The structural basis for inhibition of the classical and lectin complement pathways by S. aureus extracellular adherence protein.
P2860
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P2860
The crystal structures of EAP domains from Staphylococcus aureus reveal an unexpected homology to bacterial superantigens.
description
2005 nî lūn-bûn
@nan
2005年の論文
@ja
2005年学术文章
@wuu
2005年学术文章
@zh-cn
2005年学术文章
@zh-hans
2005年学术文章
@zh-my
2005年学术文章
@zh-sg
2005年學術文章
@yue
2005年學術文章
@zh
2005年學術文章
@zh-hant
name
The crystal structures of EAP ...... gy to bacterial superantigens.
@en
type
label
The crystal structures of EAP ...... gy to bacterial superantigens.
@en
prefLabel
The crystal structures of EAP ...... gy to bacterial superantigens.
@en
P2093
P2860
P356
P1476
The crystal structures of EAP ...... gy to bacterial superantigens.
@en
P2093
Adam Zemla
Benjamin Perman
Brent Y Hamaoka
Brian V Geisbrecht
Daniel J Leahy
P2860
P304
17243-17250
P356
10.1074/JBC.M412311200
P407
P577
2005-02-03T00:00:00Z