Middle East respiratory syndrome coronavirus spike protein receptor-binding domain (MERS-CoV RBD) (MERS-CoV RBD)

The Middle East respiratory syndrome coronavirus (MERS-CoV) spike protein receptor-binding domain (RBD) is a specialized region within the S1 subunit of the viral spike (S) glycoprotein that mediates viral entry into host cells [NIH, 2019]. It functions by specifically recognizing and binding to the human dipeptidyl peptidase 4 (DPP4, also known as CD26) receptor, which is highly expressed in the respiratory tract [NIH, 2014; NIH, 2019]. This binding event is the first and most critical step in the infection process, making the RBD a primary target for therapeutic intervention [NIH, 2019]. Neutralizing monoclonal antibodies, such as REGN3048 and m336, are designed to bind the RBD and sterically block its interaction with DPP4, thereby preventing viral attachment and subsequent membrane fusion [ASM, 2014; Frontiers, 2024]. Additionally, the RBD is a key antigen in vaccine development, as it contains the majority of neutralizing epitopes capable of eliciting a robust immune response [MDPI, 2019; NIH, 2023]. Despite its therapeutic potential, challenges such as the emergence of viral escape mutants and the theoretical risk of antibody-dependent enhancement (ADE) must be addressed in drug and vaccine design [Semanticscholar, 2019; NIH, 2019]. Understanding the structural and functional characteristics of the MERS-CoV RBD is essential for designing effective countermeasures against MERS-CoV outbreaks [NIH, 2013].

Other names

MERS-CoV S-RBDS1-RBDSpike protein S1 subunit receptor-binding domainMERS-CoV S1-RBD

The MERS-CoV RBD binds specifically to the host cell receptor dipeptidyl peptidase 4 (DPP4), facilitating viral attachment and subsequent membrane fusion for entry into the host cell [NIH, 2019]. Therapeutic agents like monoclonal antibodies bind to the RBD to sterically hinder its interaction with DPP4, thereby neutralizing the virus [ASM, 2014].