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Insights into the autotransport process of a trimeric autotransporter, Yersinia Adhesin A (YadA)
Author(s) -
Chauhan Nandini,
Hatlem Daniel,
OrwickRydmark Marcella,
Schneider Kenneth,
Floetenmeyer Matthias,
van Rossum Barth,
Leo Jack C.,
Linke Dirk
Publication year - 2019
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/mmi.14195
Subject(s) - periplasmic space , secretion , bacterial outer membrane , bacterial adhesin , yersinia , biology , cell envelope , yersinia enterocolitica , biogenesis , virulence , mutant , microbiology and biotechnology , inner membrane , bacteria , biochemistry , escherichia coli , membrane , genetics , gene
Summary Trimeric autotransporter adhesins (TAAs) are a subset of a larger protein family called the type V secretion systems. They are localized on the cell surface of Gram‐negative bacteria, function as mediators of attachment to inorganic surfaces and host cells, and thus include important virulence factors. Yersinia adhesin A (YadA) from Yersinia enterocolitica is a prototypical TAA that is used extensively to study the structure and function of the type Vc secretion system. A solid‐state NMR study of the membrane anchor domain of YadA previously revealed a flexible stretch of small residues, termed the ASSA region, that links the membrane anchor to the stalk domain. In this study, we present evidence that single amino acid proline substitutions produce two different conformers of the membrane anchor domain of YadA; one with the N‐termini facing the extracellular surface, and a second with the N‐termini located in the periplasm. We propose that TAAs adopt a hairpin intermediate during secretion, as has been shown before for other subtypes of the type V secretion system. As the YadA transition state intermediate can be isolated from the outer membrane, future structural studies should be possible to further unravel details of the autotransport process.