کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
3424066 | 1227188 | 2013 | 8 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: Negatively charged residues in the endodomain are critical for specific assembly of spike protein into murine coronavirus Negatively charged residues in the endodomain are critical for specific assembly of spike protein into murine coronavirus](/preview/png/3424066.png)
• 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