2022
DOI: 10.1016/j.biopha.2022.113368
|View full text |Cite
|
Sign up to set email alerts
|

Molecular mechanisms involved in pathogenicity of SARS-CoV-2: Immune evasion and implications for therapeutic strategies

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
3
1
1

Citation Types

0
7
0

Year Published

2022
2022
2024
2024

Publication Types

Select...
7

Relationship

0
7

Authors

Journals

citations
Cited by 8 publications
(7 citation statements)
references
References 166 publications
0
7
0
Order By: Relevance
“…SARS-CoV-2 can act at the state of induction by inducing antagonism [ 98 , 99 , 100 , 101 , 102 ]. Other mechanisms related to failure of containment of SARS-CoV-2 in the nasal mucosa have been reported [ 103 , 104 ], and more insights will be generated in the future.…”
Section: Possible Mechanisms Underlying Failure Of Containing Sars-co...mentioning
confidence: 99%
“…SARS-CoV-2 can act at the state of induction by inducing antagonism [ 98 , 99 , 100 , 101 , 102 ]. Other mechanisms related to failure of containment of SARS-CoV-2 in the nasal mucosa have been reported [ 103 , 104 ], and more insights will be generated in the future.…”
Section: Possible Mechanisms Underlying Failure Of Containing Sars-co...mentioning
confidence: 99%
“…TMPRSS2 cleaves the S-protein into its subunits S1 and S2. This leads to the exposure of the RBD on the S1 subunit of the S-protein [78] , [79] , [80] . On the other hand, the S2 domain facilitates the fusion of viral and cellular membranes by undergoing conformational changes [80] , [81] .…”
Section: Mutational Changes and Their Impactsmentioning
confidence: 99%
“…This leads to the exposure of the RBD on the S1 subunit of the S-protein [78] , [79] , [80] . On the other hand, the S2 domain facilitates the fusion of viral and cellular membranes by undergoing conformational changes [80] , [81] . It is interesting to note that the electron microscopic studies have found that the binding affinity of SARS-CoV-2 S-protein to ACE2 is approximately 10–20 times greater than that of S protein of other SARS-CoVs [80] , [82] .…”
Section: Mutational Changes and Their Impactsmentioning
confidence: 99%
See 1 more Smart Citation
“…Consecutively, the S2 domain undergoes structural modifications that assist in the union of viral and cellular membranes [ 31 , 32 ]. It is noteworthy that according to studies using electron microscopy, the SARS-CoV-2 S Protein has a binding affinity to ACE2 that is around 10–20 times larger than that of the S proteins from other SARS-CoVs [ 30 , 33 ].…”
Section: Introductionmentioning
confidence: 99%