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Front Cover: Autotransporter Adhesins in Escherichia coli Pathogenesis
Author(s) -
Vo Julieanne L.,
Martínez Ortiz Gabriela Constanza,
Subedi Pramod,
Keerthikumar Shivakumar,
Mathivanan Suresh,
Paxman Jason J.,
Heras Begoña
Publication year - 2017
Publication title -
proteomics
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.2017700181
Subject(s) - bacterial adhesin , serine protease , bacterial outer membrane , microbiology and biotechnology , proteases , escherichia coli , virulence , biology , serine , protease , biochemistry , enzyme , gene
DOI: 10.1002/pmic.201600431 Autotransporter proteins are the largest family of secreted proteins in Gram‐negative bacteria. As discussed in article number 1600431 by Julieanne L. Vo et al., this family includes outer membrane adhesins and secreted serine proteases, which promote virulence functions such as adhesion and invasion of host cells, biofilm formation and cytotoxicity. Autotransporters incorporate a membrane spanning beta‐barrel and an extracellular functional domain. This figure represents the architecture of a trimeric adhesin (YadA (1P9H, 3H7X, 2LME)); a beta‐helical adhesin (Antigen 43 functional domain and AIDA‐I beta‐barrel (4KH3, 4MEE)) and a serine protease autotransporter (Hemoglobin‐binding protease (1WXR, 3AEH)).