Dataset Information

CpaA is a Glycan-Specific Adamalysin-like Protease Secreted by Acinetobacter baumannii that Inactivates Coagulation Factor XII

ABSTRACT: Identification of protein N-terminus and o-linked glycan modifications

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Henriette Remmer

LAB HEAD: Henriette Remmer

PROVIDER: PXD011237 | Pride | 2024-02-05

REPOSITORIES: Pride

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Dataset's files

Source:

			Action	DRS
	MSB30789A.mgf_20171208_Byonic(1).pride.mgf.gz	Mgf
	MSB30789A.mgf_20171208_Byonic.mzid.gz	Mzid
	MSB30789A.mgf_20171208_Byonic.pride.mztab.gz	Mztab
	MSB30789A.mgf_20171208_Byonic_1_.mgf	Mgf
	MSB30789A.raw	Raw

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Publications

CpaA Is a Glycan-Specific Adamalysin-like Protease Secreted by Acinetobacter baumannii That Inactivates Coagulation Factor XII.

Waack Ursula U Warnock Mark M Yee Andrew A Huttinger Zachary Z Smith Sara S Kumar Ayush A Deroux Alban A Ginsburg David D Mobley Harry L T HLT Lawrence Daniel A DA Sandkvist Maria M

mBio 20181218 6

Antibiotic-resistant <i>Acinetobacter baumannii</i> is increasingly recognized as a cause of difficult-to-treat nosocomial infections, including pneumonia, wound infections, and bacteremia. Previous studies have demonstrated that the metalloprotease CpaA contributes to virulence and prolongs clotting time when added to human plasma as measured by the activated partial thromboplastin time (aPTT) assay. Here, we show that CpaA interferes with the intrinsic coagulation pathway, also called the cont ...[more]

PMID: 30563903

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