The Receptor Binding Domain of the New Middle East Respiratory Syndrome Coronavirus Maps to a 231-Residue Region in the Spike Protein That Efficiently Elicits Neutralizing Antibodies

H. Mou; V. Stalin Raj; F.J.M. van Kuppeveld; P.J.M. Rottier; B.L. Haagmans; B.J. Bosch

doi:10.1128/JVI.01277-13

The Receptor Binding Domain of the New Middle East Respiratory Syndrome Coronavirus Maps to a 231-Residue Region in the Spike Protein That Efficiently Elicits Neutralizing Antibodies

H. Mou
, V. Stalin Raj
, F.J.M. van Kuppeveld
, P.J.M. Rottier
, B.L. Haagmans
, B.J. Bosch

Faculty of Veterinary Medicine

extern

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

Abstract

The spike (S) protein of the recently emerged human Middle East respiratory syndrome coronavirus (MERS-CoV) mediates infection
by binding to the cellular receptor dipeptidyl peptidase 4 (DPP4). Here we mapped the receptor binding domain in the S
protein to a 231-amino-acid fragment (residues 358 to 588) by evaluating the interaction of spike truncation variants with receptor-
expressing cells and soluble DPP4. Antibodies to this domain—much less so those to the preceding N-terminal region—efficiently
neutralize MERS-CoV infection.

Original language	English
Pages (from-to)	9379-9383
Number of pages	5
Journal	Journal of Virology
Volume	87
Issue number	16
DOIs	https://doi.org/10.1128/JVI.01277-13
Publication status	Published - 2013

Keywords

Antibodies, Neutralizing
Antibodies, Viral
Binding Sites
Cell Line
Coronavirus
Dipeptidyl Peptidase 4
Epitopes, B-Lymphocyte
Humans
Membrane Glycoproteins
Receptors, Virus
Spike Glycoprotein, Coronavirus
Viral Envelope Proteins
Virus Attachment

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10.1128/JVI.01277-13

Mou , H. et al. J Virol 2013 Aug 87(16) 9379-9383Final published version, 785 KB

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title = "The Receptor Binding Domain of the New Middle East Respiratory Syndrome Coronavirus Maps to a 231-Residue Region in the Spike Protein That Efficiently Elicits Neutralizing Antibodies",

abstract = "The spike (S) protein of the recently emerged human Middle East respiratory syndrome coronavirus (MERS-CoV) mediates infection by binding to the cellular receptor dipeptidyl peptidase 4 (DPP4). Here we mapped the receptor binding domain in the S protein to a 231-amino-acid fragment (residues 358 to 588) by evaluating the interaction of spike truncation variants with receptor- expressing cells and soluble DPP4. Antibodies to this domain{\textemdash}much less so those to the preceding N-terminal region{\textemdash}efficiently neutralize MERS-CoV infection.",

keywords = "Antibodies, Neutralizing, Antibodies, Viral, Binding Sites, Cell Line, Coronavirus, Dipeptidyl Peptidase 4, Epitopes, B-Lymphocyte, Humans, Membrane Glycoproteins, Receptors, Virus, Spike Glycoprotein, Coronavirus, Viral Envelope Proteins, Virus Attachment",

author = "H. Mou and \{Stalin Raj\}, V. and \{van Kuppeveld\}, F.J.M. and P.J.M. Rottier and B.L. Haagmans and B.J. Bosch",

year = "2013",

doi = "10.1128/JVI.01277-13",

language = "English",

volume = "87",

pages = "9379--9383",

journal = "Journal of Virology",

issn = "0022-538X",

publisher = "American Society for Microbiology",

number = "16",

}

The Receptor Binding Domain of the New Middle East Respiratory Syndrome Coronavirus Maps to a 231-Residue Region in the Spike Protein That Efficiently Elicits Neutralizing Antibodies. / Mou, H.; Stalin Raj, V.; van Kuppeveld, F.J.M. et al.
In: Journal of Virology, Vol. 87, No. 16, 2013, p. 9379-9383.

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

TY - JOUR

T1 - The Receptor Binding Domain of the New Middle East Respiratory Syndrome Coronavirus Maps to a 231-Residue Region in the Spike Protein That Efficiently Elicits Neutralizing Antibodies

AU - Mou, H.

AU - Stalin Raj, V.

AU - van Kuppeveld, F.J.M.

AU - Rottier, P.J.M.

AU - Haagmans, B.L.

AU - Bosch, B.J.

PY - 2013

Y1 - 2013

N2 - The spike (S) protein of the recently emerged human Middle East respiratory syndrome coronavirus (MERS-CoV) mediates infection by binding to the cellular receptor dipeptidyl peptidase 4 (DPP4). Here we mapped the receptor binding domain in the S protein to a 231-amino-acid fragment (residues 358 to 588) by evaluating the interaction of spike truncation variants with receptor- expressing cells and soluble DPP4. Antibodies to this domain—much less so those to the preceding N-terminal region—efficiently neutralize MERS-CoV infection.

AB - The spike (S) protein of the recently emerged human Middle East respiratory syndrome coronavirus (MERS-CoV) mediates infection by binding to the cellular receptor dipeptidyl peptidase 4 (DPP4). Here we mapped the receptor binding domain in the S protein to a 231-amino-acid fragment (residues 358 to 588) by evaluating the interaction of spike truncation variants with receptor- expressing cells and soluble DPP4. Antibodies to this domain—much less so those to the preceding N-terminal region—efficiently neutralize MERS-CoV infection.

KW - Antibodies, Neutralizing

KW - Antibodies, Viral

KW - Binding Sites

KW - Cell Line

KW - Coronavirus

KW - Dipeptidyl Peptidase 4

KW - Epitopes, B-Lymphocyte

KW - Humans

KW - Membrane Glycoproteins

KW - Receptors, Virus

KW - Spike Glycoprotein, Coronavirus

KW - Viral Envelope Proteins

KW - Virus Attachment

U2 - 10.1128/JVI.01277-13

DO - 10.1128/JVI.01277-13

M3 - Article

C2 - 23785207

SN - 0022-538X

VL - 87

SP - 9379

EP - 9383

JO - Journal of Virology

JF - Journal of Virology

IS - 16

ER -

The Receptor Binding Domain of the New Middle East Respiratory Syndrome Coronavirus Maps to a 231-Residue Region in the Spike Protein That Efficiently Elicits Neutralizing Antibodies

Abstract

Keywords

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