Ability of the hydrophobic fusion-related external domain of a paramyxovirus F protein to act as a membrane anchor

Reay G. Paterson; Robert A. Lamb

doi:10.1016/0092-8674(87)90195-4

Ability of the hydrophobic fusion-related external domain of a paramyxovirus F protein to act as a membrane anchor

Reay G. Paterson^*, Robert A. Lamb

^*Corresponding author for this work

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

68 Scopus citations

Abstract

The hydrophobic NH₂ terminus of F₁ (FRED) of the simian virus 5 fusion (F) protein is implicated in mediating cell fusion, but in the inactive F₀ precursor the FRED is translocated across membranes. Hybrid proteins containing the FRED as a potential membrane anchorage domain and a mutant of F₀ lacking the preceding five-arginine cleavage/activation site were used to study the effect of position on the FRED. The experiments indicate that the SV5 F protein has evolved an exquisite control system for biological activity: the FRED is close to the threshold of hydrophobicity required to function as a membrane anchor. The FRED is not sufficiently hydrophobic to halt translocation when in an internal position, but on cleavage/activation the threshold of hydrophobicity is effectively lowered, and the FRED, now the NH₂ terminus of F₁, is able to interact stably with membranes.

Original language	English (US)
Pages (from-to)	441-452
Number of pages	12
Journal	Cell
Volume	48
Issue number	3
DOIs	https://doi.org/10.1016/0092-8674(87)90195-4
State	Published - Feb 13 1987

Funding

We thank Margaret Shaughnessy for excellent technical assistance, and Dr. Ching-Juh Lai for providing the pHASV40 clone and antisera to AlUdorn influenza HA. This research was supported by National institutes of Health Research Awards AI-20201 and Al-23173. R. A. L. is an Established Investigator of the American Heart Association.

ASJC Scopus subject areas

General Biochemistry, Genetics and Molecular Biology

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10.1016/0092-8674(87)90195-4

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title = "Ability of the hydrophobic fusion-related external domain of a paramyxovirus F protein to act as a membrane anchor",

abstract = "The hydrophobic NH2 terminus of F1 (FRED) of the simian virus 5 fusion (F) protein is implicated in mediating cell fusion, but in the inactive F0 precursor the FRED is translocated across membranes. Hybrid proteins containing the FRED as a potential membrane anchorage domain and a mutant of F0 lacking the preceding five-arginine cleavage/activation site were used to study the effect of position on the FRED. The experiments indicate that the SV5 F protein has evolved an exquisite control system for biological activity: the FRED is close to the threshold of hydrophobicity required to function as a membrane anchor. The FRED is not sufficiently hydrophobic to halt translocation when in an internal position, but on cleavage/activation the threshold of hydrophobicity is effectively lowered, and the FRED, now the NH2 terminus of F1, is able to interact stably with membranes.",

author = "Paterson, \{Reay G.\} and Lamb, \{Robert A.\}",

note = "Funding Information: We thank Margaret Shaughnessy for excellent technical assistance, and Dr. Ching-Juh Lai for providing the pHASV40 clone and antisera to AlUdorn influenza HA. This research was supported by National institutes of Health Research Awards AI-20201 and Al-23173. R. A. L. is an Established Investigator of the American Heart Association.",

year = "1987",

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doi = "10.1016/0092-8674(87)90195-4",

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T1 - Ability of the hydrophobic fusion-related external domain of a paramyxovirus F protein to act as a membrane anchor

AU - Paterson, Reay G.

AU - Lamb, Robert A.

N1 - Funding Information: We thank Margaret Shaughnessy for excellent technical assistance, and Dr. Ching-Juh Lai for providing the pHASV40 clone and antisera to AlUdorn influenza HA. This research was supported by National institutes of Health Research Awards AI-20201 and Al-23173. R. A. L. is an Established Investigator of the American Heart Association.

PY - 1987/2/13

Y1 - 1987/2/13

N2 - The hydrophobic NH2 terminus of F1 (FRED) of the simian virus 5 fusion (F) protein is implicated in mediating cell fusion, but in the inactive F0 precursor the FRED is translocated across membranes. Hybrid proteins containing the FRED as a potential membrane anchorage domain and a mutant of F0 lacking the preceding five-arginine cleavage/activation site were used to study the effect of position on the FRED. The experiments indicate that the SV5 F protein has evolved an exquisite control system for biological activity: the FRED is close to the threshold of hydrophobicity required to function as a membrane anchor. The FRED is not sufficiently hydrophobic to halt translocation when in an internal position, but on cleavage/activation the threshold of hydrophobicity is effectively lowered, and the FRED, now the NH2 terminus of F1, is able to interact stably with membranes.

AB - The hydrophobic NH2 terminus of F1 (FRED) of the simian virus 5 fusion (F) protein is implicated in mediating cell fusion, but in the inactive F0 precursor the FRED is translocated across membranes. Hybrid proteins containing the FRED as a potential membrane anchorage domain and a mutant of F0 lacking the preceding five-arginine cleavage/activation site were used to study the effect of position on the FRED. The experiments indicate that the SV5 F protein has evolved an exquisite control system for biological activity: the FRED is close to the threshold of hydrophobicity required to function as a membrane anchor. The FRED is not sufficiently hydrophobic to halt translocation when in an internal position, but on cleavage/activation the threshold of hydrophobicity is effectively lowered, and the FRED, now the NH2 terminus of F1, is able to interact stably with membranes.

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JO - Cell

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Ability of the hydrophobic fusion-related external domain of a paramyxovirus F protein to act as a membrane anchor

Abstract

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ASJC Scopus subject areas

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