The spike (S) glycoprotein of coronaviruses contains protrusions that will only bind to certain receptors on the host cell. Known receptors bind S1 are ACE2, angiotensin-converting enzyme 2; DPP4, dipeptidyl peptidase-4; APN, aminopeptidase N; CEACAM, carcinoembryonic antigen-related cell adhesion molecule 1; Sia, sialic acid; O-ac Sia, O-acetylated sialic acid. The spike (S) glycoprotein of coronaviruses is known to be essential in the binding of the virus to the host cell at the advent of the infection process. The spike protein is a large type I transmembrane protein containing two subunits, S1 and S2. S1 mainly contains a receptor binding domain (RBD), which is responsible for recognizing the cell surface receptor. S2 contains basic elements needed for the membrane fusion.The S protein plays key parts in the induction of neutralizing-antibody and T-cell responses, as well as protective immunity.
Monkeypox Virus (MPXV), the virus that causes monkeypox infection in both humans and animals, is a double-stranded DNA virus that has had a recent global outbreak in 2022 . MPXV belongs to the Poxviridae family of viruses . It consists of several key subunits including a surface membrane fusion protein (A29L, ~14 kDa), two separate envelope proteins (A30L ~14 kDa and H3L ~32kDa), an envelope glycoprotein, A35R ~15 kDa), a receptor glycoprotein that mimics IFN-alpha/beta (B16, ~37 kDa), a palmitoylated EEV membrane glycoprotein (C19L, ~35 kDa), a secreted IL-18 binding protein (D6L, ~14 kDa), a cell surface-binding protein (E8L, ~32 kDa), a telomere binding protein (I1L, ~36kDa), and a subunit required for DNA packaging (L1R, 18 kDa) .
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