Rotavirus NSP4 interacts with both the amino- and carboxyl-termini of caveolin-1. Academic Article

abstract

• Rotavirus NSP4 plays multiple roles in viral pathogenesis, morphogenesis and replication. We previously reported a direct interaction between full-length NSP4 and the enterotoxic peptide composed of NSP4 residues 114-135 with full-length caveolin-1, the structural protein of caveolae. Caveolin-1 forms a hairpin loop in the cytoplasmic leaflet of plasma membrane caveolae. This unique orientation results in both termini of caveolin-1 exposed to the cytoplasm. The goal of this study was to map the caveolin-1 residues that interact with NSP4 to obtain a more complete picture of this binding event. Utilizing reverse yeast two-hybrid analyses and direct peptide binding assays, the NSP4 binding site was localized to caveolin-1 residues 2-22 and 161-178, at the amino- and carboxyl-termini, respectively. However, NSP4 binding to one of the termini was sufficient for the interaction.

authors

• Schroeder, Friedhelm

published proceedings

• Virus Res

author list (cited authors)

• Mir, K. D., Parr, R. D., Schroeder, F., & Ball, J. M.

citation count

• 19

complete list of authors

• Mir, Kiran D||Parr, Rebecca D||Schroeder, Friedhelm||Ball, Judith M

publication date

• June 2007

publisher

• Elsevier  Publisher

published in

• Virus Research  Journal

keywords

• Amino Acid Sequence
• Base Sequence
• Binding Sites
• Caveolin 1
• DNA Primers
• Glycoproteins
• Humans
• In Vitro Techniques
• Molecular Sequence Data
• Peptide Fragments
• Protein Binding
• Protein Structure, Tertiary
• Recombinant Proteins
• Rotavirus
• Sequence Deletion
• Toxins, Biological
• Two-Hybrid System Techniques
• Viral Nonstructural Proteins

PubMed Central ID

• 17379346

Digital Object Identifier (DOI)

• 10.1016/j.virusres.2007.02.004

start page

• 106

end page

• 115

volume

• 126

issue

• 1-2

URL

• http://dx.doi.org/10.1016/j.virusres.2007.02.004