Abstract:
:ShdA is a large outer membrane protein of the autotransporter family whose passenger domain binds the extracellular matrix proteins fibronectin and collagen I, possibly by mimicking the host ligand heparin. The ShdA passenger domain consists of approximately 1,500 amino acid residues that can be divided into two regions based on features of the primary amino acid sequence: an N-terminal nonrepeat region followed by a repeat region composed of two types of imperfect direct amino acid repeats, called type A and type B. The repeat region bound bovine fibronectin with an affinity similar to that for the complete ShdA passenger domain, while the nonrepeat region exhibited comparatively low fibronectin-binding activity. A number of fusion proteins containing truncated fragments of the repeat region did not bind bovine fibronectin. However, binding of the passenger domain to fibronectin was inhibited in the presence of immune serum raised to one truncated fragment of the repeat region that contained repeats A2, B8, A3, and B9. Furthermore, a monoclonal antibody that specifically recognized an epitope in a recombinant protein containing the A3 repeat inhibited binding of ShdA to fibronectin.
journal_name
J Bacterioljournal_title
Journal of bacteriologyauthors
Kingsley RA,Abi Ghanem D,Puebla-Osorio N,Keestra AM,Berghman L,Bäumler AJdoi
10.1128/JB.186.15.4931-4939.2004keywords:
subject
Has Abstractpub_date
2004-08-01 00:00:00pages
4931-9issue
15eissn
0021-9193issn
1098-5530pii
186/15/4931journal_volume
186pub_type
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