tetano
Editor, Senior Moderator
Protein Sci
. 2023 Nov 23:e4843.
doi: 10.1002/pro.4843. Online ahead of print. Molecular Interactions between Perlecan LG3 and the SARS-CoV-2 spike protein RBD
Timothy E Gressett[SUP] 1 2 [/SUP], Md Lokman Hossen[SUP] 3 [/SUP], Grant Talkington[SUP] 1 2 [/SUP], Milla Volic[SUP] 1 [/SUP], Hugo Perez[SUP] 3 [/SUP], Purushottam B Tiwari[SUP] 4 [/SUP], Prem Chapagain[SUP] 3 5 [/SUP], Gregory Bix[SUP] 1 2 6 7 [/SUP]
Affiliations
Severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) has caused a global health crisis with significant clinical morbidity and mortality. While angiotensin-converting enzyme 2 (ACE2) is the primary receptor for viral entry, other cell surface and extracellular matrix proteins may also bind to the viral receptor binding domain (RBD) within the SARS-CoV-2 spike protein. Recent studies have implicated heparan sulfate proteoglycans, specifically perlecan LG3, in facilitating SARS-CoV-2 binding to ACE2. However, the role of perlecan LG3 in SARS-CoV-2 pathophysiology is not well understood. In this study, we investigated the binding interactions between the SARS-CoV-2 spike protein RBD and perlecan LG3 through molecular modeling simulations and surface plasmon resonance (SPR) experiments. Our results indicate stable binding between LG3 and SARS-CoV-2 spike protein RBD, which may potentially enhance RBD-ACE2 interactions. These findings shed light on the role of perlecan LG3 in SARS-CoV-2 infection and provide insight into SARS-CoV-2 pathophysiology and potential therapeutic strategy for COVID-19. This article is protected by copyright. All rights reserved.
Keywords: LG3; Perlecan; SARS-CoV-2; SPR; extracellular matrix; heparan sulfate proteoglycan; molecular dynamics.
. 2023 Nov 23:e4843.
doi: 10.1002/pro.4843. Online ahead of print. Molecular Interactions between Perlecan LG3 and the SARS-CoV-2 spike protein RBD
Timothy E Gressett[SUP] 1 2 [/SUP], Md Lokman Hossen[SUP] 3 [/SUP], Grant Talkington[SUP] 1 2 [/SUP], Milla Volic[SUP] 1 [/SUP], Hugo Perez[SUP] 3 [/SUP], Purushottam B Tiwari[SUP] 4 [/SUP], Prem Chapagain[SUP] 3 5 [/SUP], Gregory Bix[SUP] 1 2 6 7 [/SUP]
Affiliations
- PMID: 37996967
- DOI: 10.1002/pro.4843
Severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) has caused a global health crisis with significant clinical morbidity and mortality. While angiotensin-converting enzyme 2 (ACE2) is the primary receptor for viral entry, other cell surface and extracellular matrix proteins may also bind to the viral receptor binding domain (RBD) within the SARS-CoV-2 spike protein. Recent studies have implicated heparan sulfate proteoglycans, specifically perlecan LG3, in facilitating SARS-CoV-2 binding to ACE2. However, the role of perlecan LG3 in SARS-CoV-2 pathophysiology is not well understood. In this study, we investigated the binding interactions between the SARS-CoV-2 spike protein RBD and perlecan LG3 through molecular modeling simulations and surface plasmon resonance (SPR) experiments. Our results indicate stable binding between LG3 and SARS-CoV-2 spike protein RBD, which may potentially enhance RBD-ACE2 interactions. These findings shed light on the role of perlecan LG3 in SARS-CoV-2 infection and provide insight into SARS-CoV-2 pathophysiology and potential therapeutic strategy for COVID-19. This article is protected by copyright. All rights reserved.
Keywords: LG3; Perlecan; SARS-CoV-2; SPR; extracellular matrix; heparan sulfate proteoglycan; molecular dynamics.