Sequence and structure of the coronavirus peplomer protein.

R. J. de Groot; J. A. Lenstra; W. Luytjes; H. G. Niesters; M. C. Horzinek; B. A. van der Zeijst; W. J. Spaan

doi:10.1007/978-1-4684-1280-2_4

Sequence and structure of the coronavirus peplomer protein.

R. J. de Groot^*
, J. A. Lenstra
, W. Luytjes
, H. G. Niesters
, M. C. Horzinek
, B. A. van der Zeijst
, W. J. Spaan

^*Corresponding author for this work

Utrecht University

Research output: Chapter in Book/Report/Conference proceeding › Chapter › Academic › peer-review

Abstract

Coronaviruses display a characteristic fringe of large (17–20 nm), clubshaped peplomers, each consisting of a di- or trimer of the peplomer protein (Cavanagh et al. 1983). The peplomer protein, E2, plays an important role during the infection proces. It mediates the binding of virions to the host-cell receptors and is involved in membrane fusion. In addition, the E2 protein appears to be a major inducer of protective immunity to coronaviral infection (reviewed by Sturman and Holmes, 1983)

Original language	English
Title of host publication	Coronaviruses
Publisher	Springer
Pages	31-38
Number of pages	8
DOIs	https://doi.org/10.1007/978-1-4684-1280-2_4
Publication status	Published - 1 Dec 1987

Publication series

Name	Advances in Experimental Medicine and Biology
Publisher	Springer
Volume	218
ISSN (Print)	0065-2598

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

SDG 3 Good Health and Well-being

Keywords

Infectious Bronchitis Virus
Coiled Coil
Heptad Repeat
Mouse Hepatitis Virus
Infectious Bronchitis Virus Strain

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title = "Sequence and structure of the coronavirus peplomer protein.",

abstract = "Coronaviruses display a characteristic fringe of large (17{\textendash}20 nm), clubshaped peplomers, each consisting of a di- or trimer of the peplomer protein (Cavanagh et al. 1983). The peplomer protein, E2, plays an important role during the infection proces. It mediates the binding of virions to the host-cell receptors and is involved in membrane fusion. In addition, the E2 protein appears to be a major inducer of protective immunity to coronaviral infection (reviewed by Sturman and Holmes, 1983)",

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doi = "10.1007/978-1-4684-1280-2\_4",

language = "English",

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T1 - Sequence and structure of the coronavirus peplomer protein.

AU - de Groot, R. J.

AU - Lenstra, J. A.

AU - Luytjes, W.

AU - Niesters, H. G.

AU - Horzinek, M. C.

AU - van der Zeijst, B. A.

AU - Spaan, W. J.

PY - 1987/12/1

Y1 - 1987/12/1

N2 - Coronaviruses display a characteristic fringe of large (17–20 nm), clubshaped peplomers, each consisting of a di- or trimer of the peplomer protein (Cavanagh et al. 1983). The peplomer protein, E2, plays an important role during the infection proces. It mediates the binding of virions to the host-cell receptors and is involved in membrane fusion. In addition, the E2 protein appears to be a major inducer of protective immunity to coronaviral infection (reviewed by Sturman and Holmes, 1983)

AB - Coronaviruses display a characteristic fringe of large (17–20 nm), clubshaped peplomers, each consisting of a di- or trimer of the peplomer protein (Cavanagh et al. 1983). The peplomer protein, E2, plays an important role during the infection proces. It mediates the binding of virions to the host-cell receptors and is involved in membrane fusion. In addition, the E2 protein appears to be a major inducer of protective immunity to coronaviral infection (reviewed by Sturman and Holmes, 1983)

KW - Infectious Bronchitis Virus

KW - Coiled Coil

KW - Heptad Repeat

KW - Mouse Hepatitis Virus

KW - Infectious Bronchitis Virus Strain

UR - https://www.scopus.com/pages/publications/0023460788

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DO - 10.1007/978-1-4684-1280-2_4

M3 - Chapter

C2 - 3434437

AN - SCOPUS:0023460788

T3 - Advances in Experimental Medicine and Biology

SP - 31

EP - 38

BT - Coronaviruses

PB - Springer

ER -

Sequence and structure of the coronavirus peplomer protein.

Abstract

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UN SDGs

Keywords

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