dChan
Anonymous ID: 3bb436 Feb. 8, 2022, 12:01 p.m. No.15578985   πŸ—„οΈ.is πŸ”—kun

>>15578893

 

found HIV similarities in 2004 paper to original SARS also

this was posted yesterday

 

>>15570872 (PB)

 

>>15578904

>>15578918

 

from 2004

referencing original SARS (2003) spike similarity to HIV.

 

Theochem. 2004 May; 677(1): 73–76.

 

Published online2004 Apr 2. doi: 10.1016/j.theochem.2004.02.018

 

PMCID: PMC7141560

 

PMID: 32287546

 

Structural similarity between HIV-1 gp41 and SARS-CoV S2proteins suggests an analogous membrane fusion mechanism

 

Xue Wu Zhangβˆ— and Yee Leng Yap

 

Abstract

 

SARS-associated coronavirus (SARS-CoV) has been identified as the causal agent of a new emerging disease: severe acute respiratory syndrome (SARS). Its spike protein S2 is responsible for mediating fusion of viral and cellular membrane. In this study, we modeled the 3D structure of S2 subunit and compared this model with the core structure of gp41 from HIV-1. We found that SARS-CoV S2 and gp41 share the same two Ξ± helices, suggesting that the two viruses could follow an analogous membrane fusion mechanism. Further ligand-binding analysis showed that two inhibitors GGL and D-peptide from HIV-1 gp41 may serve as inhibitors for SARS-CoV entry.

 

Table 2

 

Structural similarity between SARS-CoV S2 and HIV-1 gp41 proteins

 

It has been shown that that there are some similar structural motifs in HIV-1 gp41 and SARS-CoV S2 protein [4], [5]: (1) N-terminal leucine/isoleucine heptad repeat sequence on residues 913–1000; (2) C-terminal leucine/isoleucine heptad repeat motif on residues 1151–1185. While our results reveal that SARS-CoV S2 and HIV gp41 share very similar helix structure on residues 879–942, these discoveries suggest a similar membrane fusion mechanism for the two viruses.

 

Naturally, a question arises: could the inhibitors for anti-HIV-1 therapy be used to fight against SARS-CoV? For example, GGL, a HIV-1 specific cell entry inhibitor that can bind to the coiled-coil core of gp41 and efficiently inhibit HIV-1 envelope-mediated cell-cell fusion [12], and another D-peptide inhibitor, which targets the gp41 coiled-coil pocket and inhibits HIV-1 entry [13]. Fig. 3 showed the binding interaction between GGL and S2 protein, the residues involved are: 901–918. Fig. 4 showed the binding interaction between D-peptide and S2 protein, the residues involved are: 899–915. This suggests GGL and D-peptide inhibitors from HIV-1 gp41 could be used as potential inhibitors for SARS-CoV entry.

 

https://www.ncbi.nlm.nih.gov/labs/pmc/articles/PMC7141560/