A single point mutation controls the cholesterol dependence of Semliki Forest virus entry and exit

Malini Vashishtha, Thomas Phalen, Marianne T. Marquardt, Jae S. Ryu, Alice C. Ng, Margaret Kielian

Research output: Contribution to journalArticle

113 Citations (Scopus)

Abstract

Membrane fusion and budding are key steps in the life cycle of all enveloped viruses. Semliki Forest virus (SFV) is an enveloped alphavirus that requires cellular membrane cholesterol for both membrane fusion and efficient exit of progeny virus from infected cells. We selected an SFV mutant, srf-3, that was strikingly independent of cholesterol for growth. This phenotype was conferred by a single amino acid change in the E1 spike protein subunit, proline 226 to serine, that increased the cholesterol independence of both srf-3 fusion and exit. The srf-3 mutant emphasizes the relationship between the role of cholesterol in membrane fusion and virus exit, and most significantly, identifies a novel spike protein region involved in the virus cholesterol requirement.

Original languageEnglish (US)
Pages (from-to)91-99
Number of pages9
JournalJournal of Cell Biology
Volume140
Issue number1
DOIs
StatePublished - Jan 12 1998

Fingerprint

Semliki forest virus
Virus Internalization
Point Mutation
Cholesterol
Membrane Fusion
Viruses
Alphavirus
Protein Subunits
Life Cycle Stages
Proline
Serine
Phenotype
Amino Acids
Membranes
Growth
Proteins

ASJC Scopus subject areas

  • Cell Biology

Cite this

A single point mutation controls the cholesterol dependence of Semliki Forest virus entry and exit. / Vashishtha, Malini; Phalen, Thomas; Marquardt, Marianne T.; Ryu, Jae S.; Ng, Alice C.; Kielian, Margaret.

In: Journal of Cell Biology, Vol. 140, No. 1, 12.01.1998, p. 91-99.

Research output: Contribution to journalArticle

Vashishtha, Malini ; Phalen, Thomas ; Marquardt, Marianne T. ; Ryu, Jae S. ; Ng, Alice C. ; Kielian, Margaret. / A single point mutation controls the cholesterol dependence of Semliki Forest virus entry and exit. In: Journal of Cell Biology. 1998 ; Vol. 140, No. 1. pp. 91-99.
@article{c8a88d8bb19740b6ab0f0fd1d8337037,
title = "A single point mutation controls the cholesterol dependence of Semliki Forest virus entry and exit",
abstract = "Membrane fusion and budding are key steps in the life cycle of all enveloped viruses. Semliki Forest virus (SFV) is an enveloped alphavirus that requires cellular membrane cholesterol for both membrane fusion and efficient exit of progeny virus from infected cells. We selected an SFV mutant, srf-3, that was strikingly independent of cholesterol for growth. This phenotype was conferred by a single amino acid change in the E1 spike protein subunit, proline 226 to serine, that increased the cholesterol independence of both srf-3 fusion and exit. The srf-3 mutant emphasizes the relationship between the role of cholesterol in membrane fusion and virus exit, and most significantly, identifies a novel spike protein region involved in the virus cholesterol requirement.",
author = "Malini Vashishtha and Thomas Phalen and Marquardt, {Marianne T.} and Ryu, {Jae S.} and Ng, {Alice C.} and Margaret Kielian",
year = "1998",
month = "1",
day = "12",
doi = "10.1083/jcb.140.1.91",
language = "English (US)",
volume = "140",
pages = "91--99",
journal = "Journal of Cell Biology",
issn = "0021-9525",
publisher = "Rockefeller University Press",
number = "1",

}

TY - JOUR

T1 - A single point mutation controls the cholesterol dependence of Semliki Forest virus entry and exit

AU - Vashishtha, Malini

AU - Phalen, Thomas

AU - Marquardt, Marianne T.

AU - Ryu, Jae S.

AU - Ng, Alice C.

AU - Kielian, Margaret

PY - 1998/1/12

Y1 - 1998/1/12

N2 - Membrane fusion and budding are key steps in the life cycle of all enveloped viruses. Semliki Forest virus (SFV) is an enveloped alphavirus that requires cellular membrane cholesterol for both membrane fusion and efficient exit of progeny virus from infected cells. We selected an SFV mutant, srf-3, that was strikingly independent of cholesterol for growth. This phenotype was conferred by a single amino acid change in the E1 spike protein subunit, proline 226 to serine, that increased the cholesterol independence of both srf-3 fusion and exit. The srf-3 mutant emphasizes the relationship between the role of cholesterol in membrane fusion and virus exit, and most significantly, identifies a novel spike protein region involved in the virus cholesterol requirement.

AB - Membrane fusion and budding are key steps in the life cycle of all enveloped viruses. Semliki Forest virus (SFV) is an enveloped alphavirus that requires cellular membrane cholesterol for both membrane fusion and efficient exit of progeny virus from infected cells. We selected an SFV mutant, srf-3, that was strikingly independent of cholesterol for growth. This phenotype was conferred by a single amino acid change in the E1 spike protein subunit, proline 226 to serine, that increased the cholesterol independence of both srf-3 fusion and exit. The srf-3 mutant emphasizes the relationship between the role of cholesterol in membrane fusion and virus exit, and most significantly, identifies a novel spike protein region involved in the virus cholesterol requirement.

UR - http://www.scopus.com/inward/record.url?scp=0031919431&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0031919431&partnerID=8YFLogxK

U2 - 10.1083/jcb.140.1.91

DO - 10.1083/jcb.140.1.91

M3 - Article

VL - 140

SP - 91

EP - 99

JO - Journal of Cell Biology

JF - Journal of Cell Biology

SN - 0021-9525

IS - 1

ER -