Receptor destroying activities of RNA viruses: Identification of the catalytic site of the influenza C virus esterase

TY - JOUR

T1 - Receptor destroying activities of RNA viruses

T2 - Identification of the catalytic site of the influenza C virus esterase

AU - Vlasak, Reinhard

AU - Palese, Peter

N1 - Funding Information: D.S. LYLES AND B.J. MCCREEDY, Bowman Gray School of Medicine of Wake Forest University, Winston-Salem, NC 27103 USA The association of the M protein and nucleocapsid (N) protein of vesicular stomatitis virus with the cytoplasmic surface of plasma membranes isolated from infected cells was examined by double label immunofluorescence. The M protein was distributed in two distinct labeling patterns. Bright, punctate labeling of M protein in plasma membranes was superimposablew ith corresponding labeling of N protein. Diffusely distributed M protein was observed in areas of the plasma membrane that were devoid of detectable N protein. Membranes prepared from cells infected with a temperature sensitive M protein mutant at the nonpermissive temperature contained the diffusely labeled M protein, but neither the punctate label for M protein nor the labeling for N protein was present. Upon temperature shift to permissive conditions, both the punctate label for M protein and labeling of N protein in membranes began to reappear. The results indicate that M protein can associate with the plasma membrane without prior binding to nucleocapsids. Furthermore, they provide a direct demonstration that the block in virus assembly in the M protein mutants results in a failure of the nucleocapsid to associate with plasma membranes, but does not prevent membrane association of M protein. (Supported by NIH grant A115892).

PY - 1988/9

Y1 - 1988/9

UR - https://www.scopus.com/pages/publications/45449122439

U2 - 10.1016/0168-1702(88)90111-6

DO - 10.1016/0168-1702(88)90111-6

M3 - Article

AN - SCOPUS:45449122439

SN - 0168-1702

VL - 11

SP - 7

JO - Virus Research

JF - Virus Research

IS - SUPPL. 1

ER -