PMID- 34731254
OWN - NLM
STAT- MEDLINE
DCOM- 20211208
LR  - 20211214
IS  - 1420-9071 (Electronic)
IS  - 1420-682X (Linking)
VI  - 78
IP  - 24
DP  - 2021 Dec
TI  - Structural and functional insights into the spike protein mutations of emerging 
      SARS-CoV-2 variants.
PG  - 7967-7989
LID - 10.1007/s00018-021-04008-0 [doi]
AB  - Since the emergence of the first case of coronavirus disease 2019 (COVID-19), 
      caused by severe acute respiratory syndrome coronavirus (SARS-CoV-2), the viral 
      genome has constantly undergone rapid mutations for better adaptation in the host 
      system. These newer mutations have given rise to several lineages/ variants of 
      the virus that have resulted in high transmission and virulence rates compared to 
      the previously circulating variants. Owing to this, the overall caseload and 
      related mortality have tremendously increased globally to > 233 million 
      infections and > 4.7 million deaths as of Sept. 28th, 2021. SARS-CoV-2, Spike (S) 
      protein binds to host cells by recognizing human angiotensin-converting enzyme 2 
      (hACE2) receptor. The viral S protein contains S1 and S2 domains that constitute 
      the binding and fusion machinery, respectively. Structural analysis of viral S 
      protein reveals that the virus undergoes conformational flexibility and 
      dynamicity to interact with the hACE2 receptor. The SARS-CoV-2 variants and 
      mutations might be associated with affecting the conformational plasticity of S 
      protein, potentially linked to its altered affinity, infectivity, and 
      immunogenicity. This review focuses on the current circulating variants 
      of SARS-CoV-2 and the structure-function analysis of key S protein mutations 
      linked with increased affinity, higher infectivity, enhanced transmission rates, 
      and immune escape against this infection.
CI  - (c) 2021. The Author(s), under exclusive licence to Springer Nature Switzerland AG.
FAU - Gupta, Deepali
AU  - Gupta D
AD  - Department of Biophysics, All India Institute of Medical Sciences, New Delhi,, 
      Delhi, 110029, India.
FAU - Sharma, Priyanka
AU  - Sharma P
AD  - Department of Microbiology, All India Institute of Medical Sciences, New Delhi,, 
      Delhi, 110029, India.
FAU - Singh, Mandeep
AU  - Singh M
AD  - Department of Biophysics, All India Institute of Medical Sciences, New Delhi,, 
      Delhi, 110029, India.
FAU - Kumar, Mukesh
AU  - Kumar M
AD  - Department of Biophysics, All India Institute of Medical Sciences, New Delhi,, 
      Delhi, 110029, India.
FAU - Ethayathulla, A S
AU  - Ethayathulla AS
AD  - Department of Biophysics, All India Institute of Medical Sciences, New Delhi,, 
      Delhi, 110029, India.
FAU - Kaur, Punit
AU  - Kaur P
AUID- ORCID: 0000-0002-7358-3716
AD  - Department of Biophysics, All India Institute of Medical Sciences, New Delhi,, 
      Delhi, 110029, India. punitkaur@aiims.edu.
LA  - eng
GR  - IWYS04/Indian Council of Medical Research/
PT  - Journal Article
PT  - Review
DEP - 20211103
PL  - Switzerland
TA  - Cell Mol Life Sci
JT  - Cellular and molecular life sciences : CMLS
JID - 9705402
RN  - 0 (Spike Glycoprotein, Coronavirus)
RN  - 0 (spike protein, SARS-CoV-2)
RN  - EC 3.4.17.23 (ACE2 protein, human)
RN  - EC 3.4.17.23 (Angiotensin-Converting Enzyme 2)
RN  - SARS-CoV-2 variants
SB  - IM
MH  - Adaptation, Physiological/genetics
MH  - Angiotensin-Converting Enzyme 2/metabolism
MH  - COVID-19/pathology/transmission
MH  - Genome, Viral/genetics
MH  - Humans
MH  - Immune Evasion/*genetics
MH  - Protein Conformation
MH  - SARS-CoV-2/*genetics/*immunology
MH  - Spike Glycoprotein, Coronavirus/*genetics/*immunology/metabolism
OTO - NOTNLM
OT  - Lineages
OT  - S protein
OT  - SARS-CoV-2
OT  - Structure-functional analysis
OT  - Variant of concern (VOC)
EDAT- 2021/11/04 06:00
MHDA- 2021/12/15 06:00
CRDT- 2021/11/03 17:24
PHST- 2021/07/08 00:00 [received]
PHST- 2021/10/22 00:00 [accepted]
PHST- 2021/10/20 00:00 [revised]
PHST- 2021/11/04 06:00 [pubmed]
PHST- 2021/12/15 06:00 [medline]
PHST- 2021/11/03 17:24 [entrez]
AID - 10.1007/s00018-021-04008-0 [pii]
AID - 10.1007/s00018-021-04008-0 [doi]
PST - ppublish
SO  - Cell Mol Life Sci. 2021 Dec;78(24):7967-7989. doi: 10.1007/s00018-021-04008-0. 
      Epub 2021 Nov 3.