کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
3424066 | 1227188 | 2013 | 8 صفحه PDF | دانلود رایگان |

• Charge-rich motif in endodomain is a major determinant for coronavirus S assembly.
• MHV exhibited different accommodations to S endodomains from other coronaviruses.
• MHV with TGEV S endodomain improved S incorporation by reverting mutation.
• MHV S assembly could be partial restored by acidic carboxy-terminal domain of N.
• Negatively charged residues in endodomain are critical for S specific assembly.
Coronavirus spike (S) protein assembles into virions via its carboxy-terminus, which is composed of a transmembrane domain and an endodomain. Here, the carboxy-terminal charge-rich motif in the endodomain was verified to be critical for the specificity of S assembly into mouse hepatitis virus (MHV). Recombinant MHVs exhibited a range of abilities to accommodate the homologous S endodomains from the betacoronaviruses bovine coronavirus and human SARS-associated coronavirus, the alphacoronavirus porcine transmissible gastroenteritis virus (TGEV), and the gammacoronavirus avian infectious bronchitis virus respectively. Interestingly, in TGEV endodomain chimeras the reverting mutations resulted in stronger S incorporation into virions, and a net gain of negatively charged residues in the charge-rich motif accounted for the improvement. Additionally, MHV S assembly could also be rescued by the acidic carboxy-terminal domain of the nucleocapsid protein. These results indicate an important role for negatively charged endodomain residues in the incorporation of MHV S protein into assembled virions.
Journal: Virology - Volume 442, Issue 1, 20 July 2013, Pages 74–81