RT info:eu-repo/semantics/article
T1 SARS-CoV-2 virus−host interaction: currently available structures and Implications of Variant Emergence on Infectivity and Immune Response
A1 Queirós Reis, Luís
A1 Gomes da Silva, Priscilla
A1 Carita Gonçalves, José Manuel
A1 Brancale, Andrea
A1 Bassetto, Marcella
A1 Mesquita, João
K1 COVID-19 (Disease)
K1 Immunology
K1 Virology
K1 SARS-CoV-2
K1 Spike protein
K1 hACE2
K1 Protein structures
K1 Proteína de pico
K1 Estructuras proteicas
K1 2420 Virología
K1 2412 Inmunología
K1 2412.10 Vacunas
AB Coronavirus disease 19, or COVID-19, is an infection associated with an unprecedented worldwide pandemic caused by the Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2), which has led to more than 215 million infected people and more than 4.5 million deaths worldwide. SARS-CoV-2 cell infection is initiated by a densely glycosylated spike (S) protein, a fusion protein, binding human angiotensin converting enzyme 2 (hACE2), that acts as the functional receptor through the receptor binding domain (RBD). In this article, the interaction of hACE2 with the RBD and how fusion is initiated after recognition are explored, as well as how mutations influence infectivity and immune response. Thus, we focused on all structures available in the Protein Data Bank for the interaction between SARS-CoV-2 S protein and hACE2. Specifically, the Delta variant carries particular mutations associated with increased viral fitness through decreased antibody binding, increased RBD affinity and altered protein dynamics. Combining both existing mutations and mutagenesis studies, new potential SARS-CoV-2 variants, harboring advantageous S protein mutations, may be predicted. These include mutations S13I and W152C, decreasing antibody binding, N460K, increasing RDB affinity, or Q498R, positively affecting both properties.
PB MDPI
YR 2021
FD 2021
LK https://uvadoc.uva.es/handle/10324/59335
UL https://uvadoc.uva.es/handle/10324/59335
LA eng
NO International Journal of Molecular Science, 2021, vol. 22, n. 19, 10836
NO Producción Científica
DS UVaDOC
RD 27-dic-2024