Recognition of Pneumococcal Peptidoglycan
نویسندگان
چکیده
منابع مشابه
Peptidoglycan Recognition Protein 3 Does Not Alter the Outcome of Pneumococcal Pneumonia in Mice
Pneumococci frequently cause community-acquired pneumonia, a disease with high mortality rates, particularly in young children and in the elderly. Endogenous antimicrobial peptides and proteins such as PGLYRP3 may contribute to the progression and outcome of this disease. Since increasing antibiotic resistant strains occur all over the world, these endogenous antimicrobial molecules are interes...
متن کاملPeptidoglycan recognition in Drosophila.
Drosophila rely primarily on innate immune responses to effectively combat a wide array of microbial pathogens. The hallmark of the Drosophila humoral immune response is the rapid production of AMPs (antimicrobial peptides) by the fat body, the insect homologue of the mammalian liver. Production of these AMPs is controlled at the level of transcription by two NF-kappaB (nuclear factor kappaB) s...
متن کاملSubstrate recognition and catalysis by LytB, a pneumococcal peptidoglycan hydrolase involved in virulence
Streptococcus pneumoniae is a major cause of life-threatening diseases worldwide. Here we provide an in-depth functional characterization of LytB, the peptidoglycan hydrolase responsible for physical separation of daughter cells. Identified herein as an N-acetylglucosaminidase, LytB is involved also in colonization and invasion of the nasopharynx, biofilm formation and evasion of host immunity ...
متن کاملStructure of the peptide network of pneumococcal peptidoglycan.
The peptide network of Streptococcus pneumoniae cell walls was solubilized using the pneumococcal autolytic amidase (N-acetylmuramoyl-L-alanine amidase, EC 3.5.1.28). The peptide material was fractionated into size classes by gel filtration followed by reverse-phase high-performance liquid chromatography which resolved the peptide population into over 40 fractions. About 40% of the lysines pres...
متن کاملStructural basis for peptidoglycan binding by peptidoglycan recognition proteins.
Peptidoglycan (PGN) recognition proteins (PGRPs) are pattern-recognition receptors of the innate immune system that bind and, in some cases, hydrolyze bacterial PGNs. We determined the crystal structure, at 2.30-A resolution, of the C-terminal PGN-binding domain of human PGRP-Ialpha in complex with a muramyl tripeptide representing the core of lysine-type PGNs from Gram-positive bacteria. The p...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Immunity
سال: 2003
ISSN: 1074-7613
DOI: 10.1016/s1074-7613(03)00205-x