Skip to content
Log in

Author

Shovon Swarnakar

View on Semantic Scholar

2 papers indexed here

We haven’t gathered this author’s papers yet. Follow them and we’ll fetch their work.

Not the right person? Other researchers publish under this name.

Open access Jul 2026

Heterogeneous binding of SARS-CoV2 fusion peptide on complex cellular membranes enhances its fusogenicity.

There are a large class of enveloped viruses that utilize sophisticated fusion mechanisms as a precursor to enter host cells. In SARS-Cov-2 the S2 domain of the S protein contains the fusion peptide (FP), which is believed to be central to the inter-membrane fusion machinery. However, the microscopic parameters that drive enhanced fusogenicity of the SARS-CoV-2 FP on realistic complex cellular membranes, leading to the observed virulence and fatality due to SARS-CoV-2 infection remains unclear. In this report, we identify the correlation between SARS-CoV-2 FP conformational and multi-phase cellular membrane dynamical heterogeneity, using existing and new membranotropic parameters, that drives enhanced SARS-CoV-2 FP fusogenicity. Combining high-resolution fluorescence microscopy and time-domain spectroscopy along with atomic molecular dynamics (MD) simulations, we demonstrate significantly enhanced membranotropy of SARS-CoV-2 FP in phase-separated model host cell membranes compared to their homogeneous counterparts. We observe dynamic phase homogenization and strongly correlated peptide-lipid diffusion, which correlates with the broader spectrum of interactions of SARS-CoV-2 FP with both the Lo and Ld, phases in the multi-phase complex model cellular membranes. Significantly, we correlate SARS-CoV-2 binding heterogeneity with lipid-mixing data to demonstrate how the FP's conformational binding landscape modulates key fusogenic parameters such as membrane fluidity and dehydration, leading to enhanced macroscopic fusion. Our findings offer a mechanistic framework that extends existing paradigms of viral fusion peptide activity to heterogeneous membrane environments, potentially informing the development of broadly acting antiviral strategies targeting the fusion machinery.

Shovon Swarnakar, Rajalakshmi Chockalingam, Sumangal Roychowdhury et al. · 0 citations
Open access Jul 2026

SARS-CoV-2 nucleocapsid protein engages with viral RNA and ERGIC lipids to drive viral core assembly

Severe acute respiratory syndrome coronavirus 2 assembles at the ER–Golgi intermediate compartment (ERGIC), yet the molecular basis of nucleocapsid (N) protein interactions with host membranes remains unclear. Using in vitro reconstituted lipid membranes and viral RNA– N complexes, we show that full-length N binds phosphatidylinositol (PI)- and phosphatidylserine (PS)-containing membranes and induces lipid clustering, an effect amplified by viral RNA and ERGIC-like membrane lipid composition. The isolated N-terminal domain lacks this activity, whereas the C-terminal domain retains membrane-associated multimerization. Although, lipid bilayers promote co-clustering of N and PI lipids, facilitating ribonucleoprotein (RNP) assembly, even on simple membranes. Importantly, ERGIC- mimicking membranes enhances this co-clustering further stabilizing RNPs of dimensions matching the viral core. In cells, viral RNA enhances N clustering without altering particle production. These findings reveal cooperative interactions between N, viral RNA, and ERGIC lipids as key drivers of lipid-dependent viral core formation, providing a mechanistic framework for the early steps of viral assembly.

Shovon Swarnakar, J. Mishra, Virgile Rat et al. · 0 citations