Aminopeptidase N is a major receptor for the enteropathogenic coronavirus TGEV

Research output: Contribution to journal › Journal article › Research › peer-review

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Aminopeptidase N is a major receptor for the enteropathogenic coronavirus TGEV. / Delmas, Bernard; Gelfi, Jaqueline; L'Haridon, René; Vogel, Lotte; Sjöström, Hans Gunnar; Norén, Ove; Laude, Hubert.

In: Nature, Vol. 357, No. 6377, 1992, p. 417-419.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Delmas, B, Gelfi, J, L'Haridon, R, Vogel, L, Sjöström, HG, Norén, O & Laude, H 1992, 'Aminopeptidase N is a major receptor for the enteropathogenic coronavirus TGEV', Nature, vol. 357, no. 6377, pp. 417-419. https://doi.org/10.1038/357417a0

APA

Delmas, B., Gelfi, J., L'Haridon, R., Vogel, L., Sjöström, H. G., Norén, O., & Laude, H. (1992). Aminopeptidase N is a major receptor for the enteropathogenic coronavirus TGEV. Nature, 357(6377), 417-419. https://doi.org/10.1038/357417a0

Vancouver

Delmas B, Gelfi J, L'Haridon R, Vogel L, Sjöström HG, Norén O et al. Aminopeptidase N is a major receptor for the enteropathogenic coronavirus TGEV. Nature. 1992;357(6377):417-419. https://doi.org/10.1038/357417a0

Author

Delmas, Bernard ; Gelfi, Jaqueline ; L'Haridon, René ; Vogel, Lotte ; Sjöström, Hans Gunnar ; Norén, Ove ; Laude, Hubert. / Aminopeptidase N is a major receptor for the enteropathogenic coronavirus TGEV. In: Nature. 1992 ; Vol. 357, No. 6377. pp. 417-419.

Bibtex

@article{9f87ac5074d011dbbee902004c4f4f50,
title = "Aminopeptidase N is a major receptor for the enteropathogenic coronavirus TGEV",
abstract = "CORONAVIRUSES, like many animal viruses, are characterized by a restricted host range and tissue tropism1. Transmissible gastroenteritis virus (TGEV), a major pathogen causing a fatal diarrhoea in newborn pig, replicates selectively in the differentiated enterocytes covering the villi of the small intestine2. To investigate the molecular determinants of the infection, we characterized the surface molecule used by the virus for binding and entry into host cells. Here we report that aminopeptidase N, an ectoenzyme abundantly expressed at the apical membrane of the enterocytes, serves as a receptor for TGEV. Monoclonal antibodies were selected for their ability to block infection by TGEV of porcine cell lines. They recognized a brush-border membrane protein of Mr, 150K, which was identified as aminopeptidase N by ammo-terminal sequencing. Two lines of evidence supported the view that the peptidase itself acts as a receptor. First, virions bound specifically to aminopep-tidase N that was purified to homogeneity. Second, recombinant expression of aminopeptidase N conferred infectivity by TGEV to an otherwise non-permissive cell line.",
author = "Bernard Delmas and Jaqueline Gelfi and Ren{\'e} L'Haridon and Lotte Vogel and Sj{\"o}str{\"o}m, {Hans Gunnar} and Ove Nor{\'e}n and Hubert Laude",
year = "1992",
doi = "10.1038/357417a0",
language = "English",
volume = "357",
pages = "417--419",
journal = "Nature",
issn = "0028-0836",
publisher = "nature publishing group",
number = "6377",

}

RIS

TY - JOUR

T1 - Aminopeptidase N is a major receptor for the enteropathogenic coronavirus TGEV

AU - Delmas, Bernard

AU - Gelfi, Jaqueline

AU - L'Haridon, René

AU - Vogel, Lotte

AU - Sjöström, Hans Gunnar

AU - Norén, Ove

AU - Laude, Hubert

PY - 1992

Y1 - 1992

N2 - CORONAVIRUSES, like many animal viruses, are characterized by a restricted host range and tissue tropism1. Transmissible gastroenteritis virus (TGEV), a major pathogen causing a fatal diarrhoea in newborn pig, replicates selectively in the differentiated enterocytes covering the villi of the small intestine2. To investigate the molecular determinants of the infection, we characterized the surface molecule used by the virus for binding and entry into host cells. Here we report that aminopeptidase N, an ectoenzyme abundantly expressed at the apical membrane of the enterocytes, serves as a receptor for TGEV. Monoclonal antibodies were selected for their ability to block infection by TGEV of porcine cell lines. They recognized a brush-border membrane protein of Mr, 150K, which was identified as aminopeptidase N by ammo-terminal sequencing. Two lines of evidence supported the view that the peptidase itself acts as a receptor. First, virions bound specifically to aminopep-tidase N that was purified to homogeneity. Second, recombinant expression of aminopeptidase N conferred infectivity by TGEV to an otherwise non-permissive cell line.

AB - CORONAVIRUSES, like many animal viruses, are characterized by a restricted host range and tissue tropism1. Transmissible gastroenteritis virus (TGEV), a major pathogen causing a fatal diarrhoea in newborn pig, replicates selectively in the differentiated enterocytes covering the villi of the small intestine2. To investigate the molecular determinants of the infection, we characterized the surface molecule used by the virus for binding and entry into host cells. Here we report that aminopeptidase N, an ectoenzyme abundantly expressed at the apical membrane of the enterocytes, serves as a receptor for TGEV. Monoclonal antibodies were selected for their ability to block infection by TGEV of porcine cell lines. They recognized a brush-border membrane protein of Mr, 150K, which was identified as aminopeptidase N by ammo-terminal sequencing. Two lines of evidence supported the view that the peptidase itself acts as a receptor. First, virions bound specifically to aminopep-tidase N that was purified to homogeneity. Second, recombinant expression of aminopeptidase N conferred infectivity by TGEV to an otherwise non-permissive cell line.

U2 - 10.1038/357417a0

DO - 10.1038/357417a0

M3 - Journal article

VL - 357

SP - 417

EP - 419

JO - Nature

JF - Nature

SN - 0028-0836

IS - 6377

ER -

ID: 297901