Activation of the Sendai virus fusion protein by receptor binding.

Abstract:

:2,3 Dehydro-2-deoxy-N-acetyl-neuraminic acid (DNANA) competitively inhibits the neuraminidase activity of Hemagglutinin-neuraminidase (HN) from Sendai virus. The inhibition constant depends on the presence of the Fusion (F) protein, which is 30 microM in the presence of active F protein and 50 microM when the F protein is inactivated. These data correlate with previously reported evidence of interaction of the F protein with HN (Dallocchio, F., Tomasi, M., & Bellini, T. (1994) Biochem. Biophys. Res. Comm. 201, 988-993). Desialyzation of erythrocytes, by Clostridium neuraminidase, lowers the hemolytic activity of SV to < 0.1% of that observed on untreated erythrocytes. However, addition of DNANA causes a concentration-dependent increase of hemolytic activity. Both HN and the F protein are required for the activation of hemolytic activity by DNANA. The affinity constant for DNANA, calculated from the activation of hemolytic activity on desialyzed erythrocytes, is 35 microM, very close to the Ki for neuraminidase activity. These data suggest that the binding of the F protein to HN, induced by the binding to HN of a substrate or a substrate analogue, causes a conformational change which activates the F protein.

authors

Dallocchio F,Tomasi M,Bellini T

doi

10.1006/bbrc.1995.1301

subject

Has Abstract

pub_date

1995-03-08 00:00:00

pages

36-41

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(85)71301-0

journal_volume

208

pub_type

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