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Titolo:
Molecular determinants of species specificity in the coronavirus receptor aminopeptidase N (CD13): Influence of N-linked glycosylation
Autore:
Wentworth, DE; Holmes, KV;
Indirizzi:
Univ Colorado, Hlth Sci Ctr, Sch Med, Dept Microbiol, Denver, CO 80262 USAUniv Colorado Denver CO USA 80262 d, Dept Microbiol, Denver, CO 80262 USA
Titolo Testata:
JOURNAL OF VIROLOGY
fascicolo: 20, volume: 75, anno: 2001,
pagine: 9741 - 9752
SICI:
0022-538X(200110)75:20<9741:MDOSSI>2.0.ZU;2-I
Fonte:
ISI
Lingua:
ENG
Soggetto:
HUMAN-IMMUNODEFICIENCY-VIRUS; DIPEPTIDYL PEPTIDASE-IV; CELL-SURFACE RECEPTOR; HUMAN CYTOMEGALOVIRUS-INFECTION; ECOTROPIC MURINE RETROVIRUSES; MEMBRANE COFACTOR PROTEIN; AMINO-ACID TRANSPORTER; ACUTE MYELOID-LEUKEMIA; CORE GLYCOSYLATION; 229E RECEPTOR;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
77
Recensione:
Indirizzi per estratti:
Indirizzo: Wentworth, DE Univ Colorado, Hlth Sci Ctr, Sch Med, Dept Microbiol, CampusBox B175,4200East 9th Ave, Denver, CO 80262 USA Univ Colorado Campus Box B175,4200 East 9th Ave Denver CO USA 80262
Citazione:
D.E. Wentworth e K.V. Holmes, "Molecular determinants of species specificity in the coronavirus receptor aminopeptidase N (CD13): Influence of N-linked glycosylation", J VIROLOGY, 75(20), 2001, pp. 9741-9752

Abstract

Aminopeptidase N (APN), a 150-kDa metalloprotease also called CD13, servesas a receptor for serologically related coronaviruses of humans (human coronavirus 229E [HCoV-229E]), pigs, and cats. These virus-receptor interactions can be highly species specific; for example, the human coronavirus can use human APN (hAPN) but not porcine APN (pAPN) as its cellular receptor, and porcine coronaviruses can use pAPN but not hAPN. Substitution of pAPN amino acids 283 to 290 into hAPN for the corresponding amino acids 288 to 295 introduced an N-glycosylation sequon at amino acids 291 to 293 that blockedHCoV-229E receptor activity of hAPN. Substitution of two amino acids that inserted an N-glycosylation site at amino acid 291 also resulted in a mutant hAPN that lacked receptor activity because it failed to hind HCoV-229E. Single amino acid revertants that removed this sequon at amino acids 291 to 293 but had one or five pAPN amino acid substitution(s) in this region all regained HCoV-229E binding and receptor activities. To determine if other N-linked glycosylation differences between hAPN, feline APN (fAPN), and pAPNaccount for receptor specificity of pig and cat coronaviruses, a mutant hAPN protein that, like fAPN and pAPN, lacked a glycosylation sequon at 818 to 820 was studied. This sequon is within the region that determines receptor activity for porcine and feline coronaviruses. Mutant hAPN lacking the sequon at amino acids 818 to 820 maintained HCoV-229E receptor activity but did not gain receptor activity for porcine or feline coronaviruses. Thus, certain differences in glycosylation between coronavirus receptors from different species are critical determinants in the species specificity of infection.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 01/12/20 alle ore 22:18:17