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 infectionby binding to the cellular receptor dipeptidyl peptidase 4 (DPP4). Here we mapped the receptor binding domain in the Sprotein 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—efficientlyneutralize MERS-CoV infection.",

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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",

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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 infectionby binding to the cellular receptor dipeptidyl peptidase 4 (DPP4). Here we mapped the receptor binding domain in the Sprotein 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—efficientlyneutralize MERS-CoV infection.

AB - The spike (S) protein of the recently emerged human Middle East respiratory syndrome coronavirus (MERS-CoV) mediates infectionby binding to the cellular receptor dipeptidyl peptidase 4 (DPP4). Here we mapped the receptor binding domain in the Sprotein 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—efficientlyneutralize 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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