Abstract:
BACKGROUND:The Bacillus anthracis S-layer protein, BslA, plays a crucial role in mammalian infection. BslA is required to mediate adherence between host cells and vegetative forms of bacteria and this interaction promotes target organs adherence and blood-brain barrier (BBB) penetration in vivo. This study attempts to identify the potential eukaryotic ligand(s) for B. anthracis BslA protein. RESULTS:Biochemical approaches have indicated that the putative host cell ligand(s) for BslA is a surface protein, which is independent of the sugar components for binding to Bs1A. A ligand screening using blot overlays, far Western blots and mass spectrometry analyses revealed that BslA binds to mammalian laminin. ELISA based solid-phase binding assays and surface plasmon resonance assays demonstrated that there were high affinity interactions between BslA(260-652) and laminin. The SPR results also revealed the dissociation constants values of 3.172 × 10(-9)M for the binding of BslA(260-652) to laminin. CONCLUSIONS:These data demonstrated that laminin is a ligand for BslA.
journal_name
BMC Microbioljournal_title
BMC microbiologyauthors
Wang Y,Wei Y,Yuan S,Tao H,Dong J,Zhang Z,Tian W,Liu Cdoi
10.1186/s12866-016-0802-8subject
Has Abstractpub_date
2016-08-11 00:00:00pages
183issue
1issn
1471-2180pii
10.1186/s12866-016-0802-8journal_volume
16pub_type
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