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Caveolin-1 binding motif of alpha-hemolysin: its role in stability and pore formation. | LitMetric

Caveolin-1 binding motif of alpha-hemolysin: its role in stability and pore formation.

Biochem Biophys Res Commun

National Centre for Cell Science, Ganeshkhind Road, Pune 411007, Maharashtra, India.

Published: September 2004

AI Article Synopsis

Article Abstract

We have identified a nine amino sequence in alpha-hemolysin (alpha-HL) of Staphylococcus aureus, which binds Caveolin-1. Surface plasmon resonance studies clearly show a concentration dependent interaction of alpha-HL with the scaffolding domain of Caveolin-1. Mutants of alpha-HL, devoid of Caveolin-1 recognition motif, exhibit an alpha-HL like proteinase K digestion profile but the resultant 'half-like' domains are highly susceptible to further proteolysis. They also had the same intrinsic fluorescence emission maxima as the native alpha-HL indicating normal folding. However, these mutants bind 1-anilino-8-naphthalene sulfonic acid probably due to exposure of their hydrophobic core. Moreover, these mutants are non-lytic and do not undergo conformational changes on rabbit RBC membrane surface. Purified Caveolin-1 blocks the hemolysis of RBCs by alpha-HL. Our studies indicate that the Caveolin-1 binding motif of alpha-HL provides stability and shields the hydrophobic core of alpha-HL. The motif also acts as trigger point for initiation of conformational changes.

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Source
http://dx.doi.org/10.1016/j.bbrc.2004.07.073DOI Listing

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