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Dissecting the Molecular Basis of Host Leucine-Rich Repeat Containing 15 Mediated Interaction with Receptor Binding

Sarbani Mishra1, Mansi Sharma2, Mahendra Kumar Singh3

  • 1Bioinformatics Division, ICMR-Regional Medical Research Centre, Nalco Square, Chandrasekharpur, Bhubaneswar 751023, Odisha, India.

The Journal of Physical Chemistry Letters
|October 2, 2023
PubMed

Insights

Leucine-rich repeat containing 15 (LRRC15) interacts with SARS-CoV-2 spike protein's RBD. Molecular simulations reveal alternative binding modes, influencing viral entry and host immunity during the COVID-19 pandemic.

Area of Science:

  • Virology
  • Structural Biology
  • Immunology

Background:

  • Leucine-rich repeat containing 15 (LRRC15) is linked to SARS-CoV-2 infection pathways.
  • The precise interaction mechanism between LRRC15 and the SARS-CoV-2 spike protein's receptor binding domain (RBD) remains unclear.

Purpose of the Study:

  • To elucidate the structure-function mechanism of LRRC15 in SARS-CoV-2 interaction.
  • To investigate the binding modes and affinities between LRRC15 and the SARS-CoV-2 RBD.

Main Methods:

  • Utilized AlphaFold2 for structural prediction.
  • Employed all-atom molecular dynamics simulations to analyze interactions.

Main Results:

  • Identified alternative binding modes of the SARS-CoV-2 RBD with LRRC15 LRR units.
  • Demonstrated varied binding affinities based on these interactions.
  • Highlighted the role of RBD's receptor binding regions in accommodating LRRC15.

Conclusions:

  • LRRC15 exhibits differential binding to SARS-CoV-2 RBD, impacting host cell receptiveness and innate immunity.
  • Findings suggest LRRC15's role in modulating antiviral tone.
  • Further experimental validation is required to fully understand LRRC15's function in COVID-19.

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