S
Sarkis K. Mazmanian
Researcher at California Institute of Technology
Publications - 161
Citations - 46119
Sarkis K. Mazmanian is an academic researcher from California Institute of Technology. The author has contributed to research in topics: Microbiome & Immune system. The author has an hindex of 68, co-authored 143 publications receiving 36491 citations. Previous affiliations of Sarkis K. Mazmanian include University of Chicago & Brigham and Women's Hospital.
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Journal ArticleDOI
Staphylococcus aureus sortase mutants defective in the display of surface proteins and in the pathogenesis of animal infections.
TL;DR: The cell wall envelope of gram-positive bacteria represents a surface organelle responsible for interactions with the host environment during the pathogenesis of bacterial infections.
Journal ArticleDOI
Gut microbiota utilize immunoglobulin A for mucosal colonization
Gregory P. Donaldson,Mark S. Ladinsky,Kristie B. Yu,Jon G. Sanders,Bryan B. Yoo,Wen-Chi Chou,Margaret E. Conner,Ashlee M. Earl,Rob Knight,Pamela J. Bjorkman,Sarkis K. Mazmanian +10 more
TL;DR: It is proposed that IgA responses can be co-opted by the microbiome to engender robust host-microbial symbiosis and mediates stable colonization of the gut through exclusion of exogenous competitors.
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Sortase-catalysed anchoring of surface proteins to the cell wall of Staphylococcus aureus.
TL;DR: Many surface proteins of Gram‐positive bacteria are anchored to the cell wall envelope by a transpeptidation mechanism, requiring a C‐terminal sorting signal with a conserved LPXTG motif, and it is conceivable that S. aureus has evolved more than one pathway for the transport of 20 surface proteins to thecell wall envelope.
Journal ArticleDOI
An iron-regulated sortase anchors a class of surface protein during Staphylococcus aureus pathogenesis
TL;DR: Cell wall-anchored surface proteins and the isd locus seem involved in a novel mechanism of iron acquisition that is important for bacterial pathogenesis.
Journal ArticleDOI
Anchoring of surface proteins to the cell wall of Staphylococcus aureus. Sortase catalyzed in vitro transpeptidation reaction using LPXTG peptide and NH(2)-Gly(3) substrates.
TL;DR: It is found that purified recombinant sortase hydrolyzed peptides bearing an LPXTG motif at the peptide bond between threonine and glycine, suggesting that sortase catalyzed the transpeptidation reaction of surface protein anchoring via the formation of a thioester acyl-enzyme intermediate.