TY - JOUR
T1 - Myristoylation-Enhanced Binding of the HIV-1 Net Protein to T Cell Skeletal Matrix
AU - Niederman, Thomas M.J.
AU - Hastings, W. Randall
AU - Ratner, Lee
PY - 1993/11
Y1 - 1993/11
N2 - The negative factor, Nef, of HIV-1 was found to associate to an extent of 16-42% with the detergent insoluble cytoskeletal fraction of T lymphocytes. Furthermore, Escherichia coli expressed Nef protein was found to bind during in vitro reactions with the cytoskeletal matrix to an extent of 30-50%. Cytoskeletal association of Nef was significantly enhanced by myristoylation. The specificity of the myristoylation-enhanced binding was demonstrated by the lack of an effect of myristoylation on binding of the HIV-1 Gag protein to the cytoskeleton. Cytoskeletal binding was saturable, and inhibited by high concentrations of sodium chloride, or with SDS or urea. Binding of Nef to the cytoskeletal matrix may be important in mediating its effects on HIV-1 replication.
AB - The negative factor, Nef, of HIV-1 was found to associate to an extent of 16-42% with the detergent insoluble cytoskeletal fraction of T lymphocytes. Furthermore, Escherichia coli expressed Nef protein was found to bind during in vitro reactions with the cytoskeletal matrix to an extent of 30-50%. Cytoskeletal association of Nef was significantly enhanced by myristoylation. The specificity of the myristoylation-enhanced binding was demonstrated by the lack of an effect of myristoylation on binding of the HIV-1 Gag protein to the cytoskeleton. Cytoskeletal binding was saturable, and inhibited by high concentrations of sodium chloride, or with SDS or urea. Binding of Nef to the cytoskeletal matrix may be important in mediating its effects on HIV-1 replication.
UR - http://www.scopus.com/inward/record.url?scp=0027496255&partnerID=8YFLogxK
U2 - 10.1006/viro.1993.1605
DO - 10.1006/viro.1993.1605
M3 - Article
C2 - 8212577
AN - SCOPUS:0027496255
VL - 197
SP - 420
EP - 425
JO - Virology
JF - Virology
SN - 0042-6822
IS - 1
ER -