Chimeric influenza virus hemagglutinin containing either the NH2 terminus or the COOH terminus of G protein of vesicular stomatitis virus is defective in transport to the cell surface

N. L. McQueen; D. P. Nayak; L. V. Jones; R. W. Compans

doi:10.1073/pnas.81.2.395

Chimeric influenza virus hemagglutinin containing either the NH₂ terminus or the COOH terminus of G protein of vesicular stomatitis virus is defective in transport to the cell surface

N. L. McQueen, D. P. Nayak, L. V. Jones, R. W. Compans

Research output: Contribution to journal › Article › peer-review

12 Scopus citations

Abstract

Chimeric cDNA clones of influenza virus hemagglutinin (HA) were constructed in which the DNA encoding either the NH₂ terminus or the COOH terminus of HA was replaced with that of a vesicular stomatitis virus G protein. The chimeric cDNAs (GHA or HAG) were expressed in CV1 cells using the simian virus 40 late replacement promoter. Both chimeric proteins are synthesized, glycosylated, and transported to the rough endoplasmic reticulum. These results show that the NH₂-terminal sequences of vesicular stomatitis virus G protein can provide a signal function for translocation and the COOH-terminal sequences can provide the anchor function for the influenza virus HA, when substituted for similar sequences. However, the chimeric glycoproteins were not transported to the Golgi complex or the plasma membrane. The implication of these results in translocation, sorting, and transport processes is discussed.

Original language	English (US)
Pages (from-to)	395-399
Number of pages	5
Journal	Proceedings of the National Academy of Sciences of the United States of America
Volume	81
Issue number	2 I
DOIs	https://doi.org/10.1073/pnas.81.2.395
State	Published - 1984
Externally published	Yes

ASJC Scopus subject areas

General

Access to Document

10.1073/pnas.81.2.395

Cite this

McQueen, N. L., Nayak, D. P., Jones, L. V., & Compans, R. W. (1984). Chimeric influenza virus hemagglutinin containing either the NH₂ terminus or the COOH terminus of G protein of vesicular stomatitis virus is defective in transport to the cell surface. Proceedings of the National Academy of Sciences of the United States of America, 81(2 I), 395-399. https://doi.org/10.1073/pnas.81.2.395

Chimeric influenza virus hemagglutinin containing either the NH₂ terminus or the COOH terminus of G protein of vesicular stomatitis virus is defective in transport to the cell surface. / McQueen, N. L.; Nayak, D. P.; Jones, L. V. et al.
In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 81, No. 2 I, 1984, p. 395-399.

Research output: Contribution to journal › Article › peer-review

McQueen, NL, Nayak, DP, Jones, LV & Compans, RW 1984, 'Chimeric influenza virus hemagglutinin containing either the NH₂ terminus or the COOH terminus of G protein of vesicular stomatitis virus is defective in transport to the cell surface', Proceedings of the National Academy of Sciences of the United States of America, vol. 81, no. 2 I, pp. 395-399. https://doi.org/10.1073/pnas.81.2.395

@article{4e5ca2b5addf4d458d091b803fe2b88d,

title = "Chimeric influenza virus hemagglutinin containing either the NH2 terminus or the COOH terminus of G protein of vesicular stomatitis virus is defective in transport to the cell surface",

abstract = "Chimeric cDNA clones of influenza virus hemagglutinin (HA) were constructed in which the DNA encoding either the NH2 terminus or the COOH terminus of HA was replaced with that of a vesicular stomatitis virus G protein. The chimeric cDNAs (GHA or HAG) were expressed in CV1 cells using the simian virus 40 late replacement promoter. Both chimeric proteins are synthesized, glycosylated, and transported to the rough endoplasmic reticulum. These results show that the NH2-terminal sequences of vesicular stomatitis virus G protein can provide a signal function for translocation and the COOH-terminal sequences can provide the anchor function for the influenza virus HA, when substituted for similar sequences. However, the chimeric glycoproteins were not transported to the Golgi complex or the plasma membrane. The implication of these results in translocation, sorting, and transport processes is discussed.",

author = "McQueen, {N. L.} and Nayak, {D. P.} and Jones, {L. V.} and Compans, {R. W.}",

year = "1984",

doi = "10.1073/pnas.81.2.395",

language = "English (US)",

volume = "81",

pages = "395--399",

journal = "Proceedings of the National Academy of Sciences of the United States of America",

issn = "0027-8424",

publisher = "National Academy of Sciences",

number = "2 I",

}

TY - JOUR

T1 - Chimeric influenza virus hemagglutinin containing either the NH2 terminus or the COOH terminus of G protein of vesicular stomatitis virus is defective in transport to the cell surface

AU - McQueen, N. L.

AU - Nayak, D. P.

AU - Jones, L. V.

AU - Compans, R. W.

PY - 1984

Y1 - 1984

N2 - Chimeric cDNA clones of influenza virus hemagglutinin (HA) were constructed in which the DNA encoding either the NH2 terminus or the COOH terminus of HA was replaced with that of a vesicular stomatitis virus G protein. The chimeric cDNAs (GHA or HAG) were expressed in CV1 cells using the simian virus 40 late replacement promoter. Both chimeric proteins are synthesized, glycosylated, and transported to the rough endoplasmic reticulum. These results show that the NH2-terminal sequences of vesicular stomatitis virus G protein can provide a signal function for translocation and the COOH-terminal sequences can provide the anchor function for the influenza virus HA, when substituted for similar sequences. However, the chimeric glycoproteins were not transported to the Golgi complex or the plasma membrane. The implication of these results in translocation, sorting, and transport processes is discussed.

AB - Chimeric cDNA clones of influenza virus hemagglutinin (HA) were constructed in which the DNA encoding either the NH2 terminus or the COOH terminus of HA was replaced with that of a vesicular stomatitis virus G protein. The chimeric cDNAs (GHA or HAG) were expressed in CV1 cells using the simian virus 40 late replacement promoter. Both chimeric proteins are synthesized, glycosylated, and transported to the rough endoplasmic reticulum. These results show that the NH2-terminal sequences of vesicular stomatitis virus G protein can provide a signal function for translocation and the COOH-terminal sequences can provide the anchor function for the influenza virus HA, when substituted for similar sequences. However, the chimeric glycoproteins were not transported to the Golgi complex or the plasma membrane. The implication of these results in translocation, sorting, and transport processes is discussed.

UR - http://www.scopus.com/inward/record.url?scp=0021349685&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0021349685&partnerID=8YFLogxK

U2 - 10.1073/pnas.81.2.395

DO - 10.1073/pnas.81.2.395

M3 - Article

C2 - 6320186

AN - SCOPUS:0021349685

SN - 0027-8424

VL - 81

SP - 395

EP - 399

JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

IS - 2 I

ER -

Chimeric influenza virus hemagglutinin containing either the NH₂ terminus or the COOH terminus of G protein of vesicular stomatitis virus is defective in transport to the cell surface

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this