Viral protein-human protein


Last updated: 2021 Aug 2
Total hit(s): 27
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Molecular interaction studies of SARS-CoV-2 RBD with different variants of hACE2. No major divergence of the interaction interface of SARS-CoV-2 RBD with hACE2
32410735
(Biochem Biophys Res Commun)
PMID
32410735
Date of Publishing: 2020 Jun 30
Title Interaction of the spike protein RBD from SARS-CoV-2 with ACE2: Similarity with SARS -Cov , hot-spot analysis and effect of the receptor polymorphism
Author(s) nameOthman H, Bouslama Z et al.
Journal Biochem Biophys Res Commun
Impact factor
2.73
Citation count: 27
Date of Entry 2021 Aug 2


Heparin binding accelerates the aggregation of pathological amyloid proteins in the brain. Comparative study to the docking score of SARS-CoV-2 S1-heparin complex to amyloid forming proteins shows molecular interaction of the SARS-COV-2 Spike S1 RBD and Heparin shows a high docking score of -282.57. By targeting the binding and aggregation process of the S1 and Heparin, neurodegenration can be prevented.
33789211
(Biochem Biophys Res Commun)
PMID
33789211
Date of Publishing: 2021 May 21
Title SARS-CoV-2 spike protein interactions with amyloidogenic proteins: Potential clues to neurodegeneration
Author(s) name Idrees D, Kumar V.
Journal Biochem Biophys Res Commun
Impact factor
2.73
Citation count: 1
Date of Entry 2021 Aug 12


SARS-CoV-2 S1 RBD binds heparin binding proteins including A, -synuclein, tau, prion, and TDP-43 RRM. The heparin binding site of S1 protein assists the binding to amyloid proteins to the viral surface and initate aggregation of these proteins, leading to neurodegenration in brain. This provides a reasonable explanation for the neurodegenerative distresses caused by a COVID infection. Increase in Kd as the temperature increased from 25 C to 40 C, showed a decrease in binding affinity for SARS-CoV-2 S1 protein complexes.
Increase in temperature usually disrupts the noncovalent interactions between a protein-protein complex, but, the decrease in binding affinity across the temperatures was less apparent for the -Syn complex with S1. This anomaly suggests a stable interaction between -synuclein to SARS-CoV-2 S1 protein.
33789211
(Biochem Biophys Res Commun)
PMID
33789211
Date of Publishing: 2021 May 21
Title SARS-CoV-2 spike protein interactions with amyloidogenic proteins: Potential clues to neurodegeneration
Author(s) name Idrees D, Kumar V.
Journal Biochem Biophys Res Commun
Impact factor
2.73
Citation count: 1
Date of Entry 2021 Aug 12


Molecular interaction studies of SARS-CoV-2 RBD with different variants of hACE2. No major divergence of the interaction interface of SARS-CoV-2 RBD with hACE2
Title Interaction of the spike protein RBD from SARS-CoV-2 with ACE2: Similarity with SARS -Cov , hot-spot analysis and effect of the receptor polymorphism
Date of Entry 2021 Jul 28


Molecular interaction studies of RBD from SARS-CoV-2 and SARS-CoV with different ACE2 orthologues Q493 might be responsible forhigher affinity due to a better satisfaction of the Van der Waals by the longer polar side chain of asparagine.
32410735
(Biochem Biophys Res Commun)
PMID
32410735
Date of Publishing: 2020 Jun 30
Title Interaction of the spike protein RBD from SARS-CoV-2 with ACE2: Similarity with SARS -Cov , hot-spot analysis and effect of the receptor polymorphism
Author(s) nameOthman H, Bouslama Z et al.
Journal Biochem Biophys Res Commun
Impact factor
2.73
Citation count: 27
Date of Entry 2021 Jul 28


Molecular interaction studies of RBD from SARS-CoV-2 and SARS-CoV with different ACE2 orthologues Q493 might be responsible forhigher affinity due to a better satisfaction of the Van der Waals by the longer polar side chain of asparagine.
32410735
(Biochem Biophys Res Commun)
PMID
32410735
Date of Publishing: 2020 Jun 30
Title Interaction of the spike protein RBD from SARS-CoV-2 with ACE2: Similarity with SARS -Cov , hot-spot analysis and effect of the receptor polymorphism
Author(s) nameOthman H, Bouslama Z et al.
Journal Biochem Biophys Res Commun
Impact factor
2.73
Citation count: 27
Date of Entry 2021 Jul 28


Molecular interaction studies of SARS-CoV-2 RBD with different variants of hACE2. No major divergence of the interaction interface of SARS-CoV-2 RBD with hACE2
Title Interaction of the spike protein RBD from SARS-CoV-2 with ACE2: Similarity with SARS -Cov , hot-spot analysis and effect of the receptor polymorphism
Date of Entry 2021 Jul 28


Molecular interaction study between polymorphic spike protein and human ACE2 The variants in the spike protein of SARS-CoV-2 and hACE2 would provide a database for tracking the adaptive mutation of SARS-CoV-2 and potential recombination events across different species.
33542420
(Sci Rep)
PMID
33542420
Date of Publishing: 2021 Feb 4
Title Dynamics of binding ability prediction between spike protein and human ACE2 reveals the adaptive strategy of SARS-CoV-2 in humans
Author(s) nameXue X, Shi J et al.
Journal Sci Rep
Impact factor
4.12
Citation count: 1
Date of Entry 2021 Jul 28


Molecular interaction of B6 (monoclonal antibody) and spike protein of SARS-CoV-2. B6 binding sterically interferes with S fusogenic conformational changes and blocks viral entry through inhibition of membrane fusion
33981021
(Nat Struct Mol Biol)
PMID
33981021
Date of Publishing: 2021 May 12
Title Structural basis for broad coronavirus neutralization
Author(s) nameSauer MM, Tortorici MA et al.
Journal Nat Struct Mol Biol
Impact factor
9.8
Citation count: 5
Date of Entry 2021 Jul 28


Surface plasmon resonance (SPR) was used to compare the kinetics of SARS-CoV-2 S protein both D614 and D614G binding to human ACE2. D614G decreases the affinity for ACE2 by increasing the rate of dissociation. The increased infectivity of D614G is not explained by greater ACE2 binding strength.
32991842
(Cell)
PMID
32991842
Date of Publishing: 2020 Oct 29
Title Structural and Functional Analysis of the D614G SARS-CoV-2 Spike Protein Variant
Author(s) nameYurkovetskiy L, Wang X et al.
Journal Cell
Impact factor
27.35
Citation count: 52
Date of Entry 2021 Jun 15


Complex of ACE2 receptor and N501Y spike protein ectodomains shows Y501 inserted into a cavity at the binding interface near Y41 of ACE2 providing a structural explanation for the increased ACE2 affinity of the N501Y mutant, and its increased infectivity, but the mutation does note cause large structural changes. Structural studies establish the molecular basis showing the increase in ACE2 binding efficiency conferred by the N501Y mutation. Despite the higher infectivity of SARS-CoV-2 viruses carrying the N501Y mutation, the availability of the extended epitope surface on the RBD enables effective neutralization by VH ab8 and Fab ab1.
33914735
(PLoS Biol)
PMID
33914735
Date of Publishing: 2021 Apr 29
Title Cryo-electron microscopy structures of the N501Y SARS-CoV-2 spike protein in complex with ACE2 and 2 potent neutralizing antibodies
Author(s) nameZhu X, Mannar D et al.
Journal PLoS Biol
Impact factor
7.62
Citation count: 2


Molecular docking study to determine the potential binding interfaces of SARS-CoV-2 ORF7a with leukocyte marker - LFA-1 (lymphocyte function-associated antigen) and Mac-1 ( Macrophage-1 antigen ) ORF7a-mediated effects on immune cells such as T lymphocytes and macrophages (leukocytes) could help understand the disease further and develop effective treatments.
33305306
(Biosci Rep)
PMID
33305306
Date of Publishing: 2020 Dec 11
Title Structural assessment of SARS-CoV2 accessory protein ORF7a predicts LFA-1 and Mac-1 binding potential
Author(s) nameNizamudeen ZA, Xu ER et al.
Journal Biosci Rep
Impact factor
2.51
Citation count: 1


Reporting strong interaction between S2 subunit of SARS-nCoV-2 with tumor suppressor protein p53 Further experimental research is required to unveil the impact of COVID-19 in cancer patients and to explore the functional role of these interactions.
32619819
(Transl Oncol)
PMID
32619819
Date of Publishing: 2020 Oct
Title S2 Subunit of SARS-nCoV-2 Interacts with Tumor Suppressor Protein p53 and BRCA: an In Silico Study
Author(s) name Singh N, Bharara Singh A.
Journal Transl Oncol
Impact factor
3.3
Citation count: 4


Reporting strong interaction between S2 subunit of SARS-nCoV-2 with tumor suppressor protein BRCA-1 Further experimental research is required to unveil the impact of COVID-19 in cancer patients and to explore the functional role of these interactions.
32619819
(Transl Oncol)
PMID
32619819
Date of Publishing: 2020 Oct
Title S2 Subunit of SARS-nCoV-2 Interacts with Tumor Suppressor Protein p53 and BRCA: an In Silico Study
Author(s) name Singh N, Bharara Singh A.
Journal Transl Oncol
Impact factor
3.3
Citation count: 4


Reporting strong interaction between S2 subunit of SARS-nCoV-2 with tumor suppressor protein BRCA-2 Further experimental research is required to unveil the impact of COVID-19 in cancer patients and to explore the functional role of these interactions.
32619819
(Transl Oncol)
PMID
32619819
Date of Publishing: 2020 Oct
Title S2 Subunit of SARS-nCoV-2 Interacts with Tumor Suppressor Protein p53 and BRCA: an In Silico Study
Author(s) name Singh N, Bharara Singh A.
Journal Transl Oncol
Impact factor
3.3
Citation count: 4


Molecular interactions of SARS-CoV-2 S protein's RBD with ACE2 receptor and CR3022. SARS-CoV-2 has a conserved, epitope shared between SARS-CoV-2 and SARS-CoV. The availability of conserved epitopes would allow structure-based design of a SARS-CoV-2 vaccine and also of cross-protective antibody responses against future coronavirus epidemics and pandemics.
32245784
(Science)
PMID
32245784
Date of Publishing: 2020 May 8
Title A highly conserved cryptic epitope in the receptor binding domains of SARS-CoV-2 and SARS-CoV
Author(s) nameYuan M, Wu NC et al.
Journal Science
Impact factor
20.57
Citation count: 269


Proving that interaction between SARS-CoV-2-CTD and hACE2 Is specific and displays 4-fold stronger affinity compared with the SARS-RBD by real-time surface plasmon resonance (SPR) assays. hACE2 and SARS-CoV-2-CTD binding region leads to ~4-fold higher binding affinity compared with the SARS-RBD. Distinct epitope features between SARS-RBD and SARS-CoV-2-CTD have been , although both can engage hACE2.
32275855
(Cell)
PMID
32275855
Date of Publishing: 2020 May 14
Title Structural and functional basis of SARS-CoV-2 entry by using human ACE2
Author(s) nameWang Q, Zhang Y et al.
Journal Cell
Impact factor
27.35
Citation count: 447


Characterization of binding between SARS-CoV-2 and hACE2 and comparative studies of the SARS-CoV-2-CTD/hACE2 and SARS-RBD/hACE2 binding sites. The virus-receptor engagement is dominated by polar contacts mediated by the hydrophilic residues. A single K353A mutation was sufficient to abolish these interactions.
32275855
(Cell)
PMID
32275855
Date of Publishing: 2020 May 14
Title Structural and functional basis of SARS-CoV-2 entry by using human ACE2.
Author(s) nameWang Q, Zhang Y et al.
Journal Cell
Impact factor
27.35
Citation count: 447


Structural characterisation of SARS-CoV-2 chimeric receptor-binding domain complexed with its receptor human ACE2 Neutralizing monoclonal antibodies targeting SARS-CoV-2 RBM can prevent the virus from binding to hACE2, and hence are promising antiviral drugs. The functionally important epitopes in SARS-CoV-2 RBM, can guide structure-based design of highly efficacious RBD vaccines.
32225175
(Nature)
PMID
32225175
Date of Publishing: 2020 May
Title Structural basis of receptor recognition by SARS-CoV-2
Author(s) nameShang J, Ye G et al.
Journal Nature
Impact factor
24.36
Citation count: 599


Molecular interactions between gangliosides and the NTD of SARS-CoV-2 S protein. CLQ and CLQ-OH, it is the nitrogen-containing ring of the drug that stacks on to the Glc ring. If once, two CLQ-OH (or two CLQ) molecules are bound to a ganglioside , any binding of a SARS-CoV-2 S protein to the same ganglioside is totally prevented. Mechanism of action of hydroxychloroquine (CLQ-OH).
32251731
(Int J Antimicrob Agents)
PMID
32251731
Date of Publishing: 2020 May
Title Structural and molecular modelling studies reveal a new mechanism of action of chloroquine and hydroxychloroquine against SARS-CoV-2 infection
Author(s) nameFantini J, Di Scala C et al.
Journal Int J Antimicrob Agents
Impact factor
4.6
Citation count: 118


The critical human ACE2-binding residues of SARS-CoV-2 RBD are L(455), GVEG (482-485), F (486), Q (493), S (494), N (501) Both structural and biochemical data reveal that SARS-CoV-2 RBD recognizes hACE2 better than SARS-CoV RBD does.
32225175
(Nature)
PMID
32225175
Date of Publishing: 2020 May
Title Structural basis of receptor recognition by SARS-CoV-2
Author(s) nameShang J, Ye G et al.
Journal Nature
Impact factor
24.36
Citation count: 599


Structural characterization of the SARS-CoV-2 receptor-binding domain of Spike glycoprotein in complex with host Cell receptor ACE2 Sequence mapping of (m396 and 80R) neutralizing antibodies with SARS-CoV-2 RBD showd no significant binding.
32225176
(Nature)
PMID
32225176
Date of Publishing: 2020 May
Title Structure of the SARS-CoV-2 spike receptor-binding domain bound to the ACE2 receptor
Author(s) nameLan J, Ge J et al.
Journal Nature
Impact factor
24.36
Citation count: 685


Comparative molecular interaction study of hACE2 and Spike glycoprotein of SARS-CoV and SARS-CoV-2. The binding affinity of SARS-CoV for hACE2 correlates with the overall rate of viral replication in distinct species. The conservation of many key contact residues could explain the similar binding affinities of SARS-CoV-2 SB and SARS-CoV SB for hACE2.
32155444
(Cell)
PMID
32155444
Date of Publishing: 2020 Apr 16
Title Structure, Function, and Antigenicity of the SARS-CoV-2 Spike Glycoprotein
Author(s) nameWalls AC, Park YJ et al.
Journal Cell
Impact factor
27.35
Citation count: 1310


Structural characterization of SARS-CoV-2 RBD-ACE2-BAT1 complex in closed conformation Superimposition of the RBD in the complex of SARS-CoV (SARS-CoV-RBD) and ACE2-PD [PDB: 2AJF] with the RBD in 6M17 ternary complex shows that the SARSCoV-2 RBD (SARS-CoV-2-RBD) is similar to SARS-CoV-RBD. Despite the overall similarity, At the N terminus of a1, the variations Arg426Asn439, Tyr484Gln498, and Thr487Asn501 at equivalent positions are observed between SARS-CoVRBD and SARS-CoV-2-RBD. The most prominent alteration is the substitution of Val404 in the SARS-CoV-RBD with Lys417 in the SARS-CoV-2-RBD. SARS-CoV-RBD to SARS-CoV-2- RBD, the substitution of interface residues Tyr442Leu455, Leu443Phe456, Phe460Tyr473, and Asn479Gln493 may also change the affinity for ACE2. At the C terminus of alpha1, Leu472 in the SARS-CoV-RBD is replaced by Phe486 in the SARS-CoV-2-RBD
32132184
(Science)
PMID
32132184
Date of Publishing: 2020 Mar 27
Title Structural basis for the recognition of SARS-CoV-2 by full-length human ACE2
Author(s) nameYan R, Zhang Y et al.
Journal Science
Impact factor
20.57
Citation count: 957


Molecular interaction and kinetics of 2019-nCoV S and angiotensin-converting enzyme 2 (ACE2) The high affinity of 2019-nCoV S for human ACE2 may contribute to the apparent ease with which 2019-nCoV can spread from human to human, however additional studies are needed to investigate this possibility.
32075877
(Science)
PMID
32075877
Date of Publishing: 2020 Mar 13
Title Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation
Author(s) nameWrapp D, Wang N et al.
Journal Science
Impact factor
20.57
Citation count: 1471