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Distintos estados conformacionales de la proteína del pico del SARS-CoV-2
Yongfei Cai1,2, Jun Zhang1,2, Tianshu Xiao1,2
1Division of Molecular Medicine, Boston Children's Hospital, Boston, MA 02115, USA.
Science (New York, N.Y.)
|July 23, 2020
Resumen
Los conocimientos estructurales sobre la proteína del pico del SARS-CoV-2 revelan sus estados de prefusión y postfusión. Comprender estas conformaciones, independientemente de las células objetivo, ayuda en el desarrollo de vacunas y terapias contra el virus.
Área de la Ciencia:
- Biología estructural
- Virología
- Inmunología
Sus antecedentes:
- La pandemia del coronavirus 2 del síndrome respiratorio agudo severo (SARS-CoV-2) requiere estrategias de intervención efectivas.
- La proteína del pico viral (S) es crucial para la entrada del SARS-CoV-2 en las células huésped a través de la fusión de la membrana.
Objetivo del estudio:
- Determinar la base estructural de la función de la proteína S del SARS-CoV-2.
- Para aclarar las conformaciones de prefusión y postfusión de la proteína S de longitud completa.
Principales métodos:
- Se utilizó la criomicroscopia electrónica (Cryo-EM) para obtener estructuras de alta resolución.
- Se analizaron dos conformaciones distintas de la proteína S: prefusión y postfusión.
Principales resultados:
- El trímero de proteína S de prefusión exhibe una conformación con dominios de unión al receptor apretados.
- La estructura posterior a la fusión revela una disposición distinta, independiente de las células objetivo.
- Los glicanos ligados al N decoran estratégicamente la estructura posterior a la fusión, ofreciendo potencialmente protección.
Conclusiones:
- El estudio proporciona una comprensión a nivel atómico de los cambios conformacionales de la proteína S del SARS-CoV-2 durante la entrada viral.
- Estos hallazgos estructurales pueden informar el diseño de nuevas vacunas y terapias antivirales dirigidas al SARS-CoV-2.
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