Literature detail

Spiking the MERS-coronavirus receptor.

Berend Jan Bosch¹ V Stalin Raj Bart L Haagmans

Affiliations 1 institutions

Virology Division, Department of Infectious Diseases & Immunology, Faculty of Veterinary Medicine, Utrecht University, 3508 TD Utrecht, the Netherlands.

PMID 23938293 2013 Cell Res eng ppublish

Article

Publication summary

A novel coronavirus, the Middle East respiratory syndrome coronavirus, recently emerged through zoonotic transmission, causing a severe lower respiratory tract infection in humans. In two recent papers, one published in Cell Research, the crystal structure of the viral receptor-binding domain in complex with the host CD26/dipeptidyl peptidase 4 receptor has now been characterized.

Virus Attachment Animals Coronavirus Dipeptidyl Peptidase 4 Humans Receptors, Virus Viral Proteins

Structured evidence records

Evidence records

2 total

Receptor Usage 1 records

Receptor Usage Extraction confidence 0.95

Key finding

The Middle East respiratory syndrome coronavirus binds to the human CD26/dipeptidyl peptidase 4 receptor via its receptor-binding domain, as shown by crystal structure analysis.

Virus

Host

Location

Supporting text

The crystal structure of the viral receptor-binding domain in complex with the host CD26/dipeptidyl peptidase 4 receptor has now been characterized.

Method: crystal structure analysis
Receptors: CD26/dipeptidyl peptidase 4

Spillover Event 1 records

Spillover Event Extraction confidence 0.80

Key finding

Middle East respiratory syndrome coronavirus (MERS-CoV) infected humans following zoonotic transmission from an animal source, representing a documented animal-to-human spillover event.

Virus

Host

Location

Supporting text

A novel coronavirus, the Middle East respiratory syndrome coronavirus, recently emerged through zoonotic transmission, causing a severe lower respiratory tract infection in humans.

Study design: unknown
Transmission direction: animal-to-human
Geographic raw: Middle East

Citation context

References

10 references

Reference network

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PMID 23075143	N Engl J Med. 2013. pp. 1814–1820	Zaki	2013
-	who	Source WHO ( ( http://www.who.int/csr/do	-
PMID 23785207 In OmniVira	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	2013
PMID 23486063	Nature. 2013. pp. 251–254	Raj	2013
PMID 12647932	Eur J Cell Biol. 2003. pp. 53–73	Boonacker	2003
-	MBio. 2012. pp. e00515–e00512	Müller	2012
PMID 23835475 In OmniVira	Structure of MERS-CoV spike receptor-binding domain complexed with human receptor DPP4.	Wang	2013
PMID 23831647 In OmniVira	Molecular basis of binding between novel human coronavirus MERS-CoV and its receptor CD26.	Lu	2013
PMID 12483204	Nat Struct Biol. 2003. pp. 19–25	Rasmussen	2003
PMID 15791205	EMBO J. 2005. pp. 1634–1643	Li	2005

Evidence overview

Evidence 2

Types 2

Virus 1

Host 1

Evidence types

Receptor Usage 1 Spillover Event 1

Linked entities

Viruses

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Locations

Publication metadata

Journal: Cell research
Volume / Issue / Pages: 23 / 9 / 1069-70
ISSN: 1748-7838
Journal country: England
DOI: 10.1038/cr.2013.108