Abstract:
:Vibrio cholerae is a bacterial pathogen that colonizes the chitinous exoskeleton of zooplankton as well as the human gastrointestinal tract. Colonization of these different niches involves an N-acetylglucosamine binding protein (GbpA) that has been reported to mediate bacterial attachment to both marine chitin and mammalian intestinal mucin through an unknown molecular mechanism. We report structural studies that reveal that GbpA possesses an unusual, elongated, four-domain structure, with domains 1 and 4 showing structural homology to chitin binding domains. A glycan screen revealed that GbpA binds to GlcNAc oligosaccharides. Structure-guided GbpA truncation mutants show that domains 1 and 4 of GbpA interact with chitin in vitro, whereas in vivo complementation studies reveal that domain 1 is also crucial for mucin binding and intestinal colonization. Bacterial binding studies show that domains 2 and 3 bind to the V. cholerae surface. Finally, mouse virulence assays show that only the first three domains of GbpA are required for colonization. These results explain how GbpA provides structural/functional modular interactions between V. cholerae, intestinal epithelium and chitinous exoskeletons.
journal_name
PLoS Pathogjournal_title
PLoS pathogensauthors
Wong E,Vaaje-Kolstad G,Ghosh A,Hurtado-Guerrero R,Konarev PV,Ibrahim AF,Svergun DI,Eijsink VG,Chatterjee NS,van Aalten DMdoi
10.1371/journal.ppat.1002373subject
Has Abstractpub_date
2012-01-01 00:00:00pages
e1002373issue
1eissn
1553-7366issn
1553-7374pii
PPATHOGENS-D-11-01931journal_volume
8pub_type
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