Scavenger receptor class B member 2 (SCARB2) (SCARB2)

Scavenger receptor class B member 2 (SCARB2), also known as LIMP-2, is a type II transmembrane protein primarily localized in the lysosomal membrane, where it plays a vital role in maintaining lysosomal health and organizing the endosomal compartment (Wikipedia, https://en.wikipedia.org/wiki/SCARB2; NIH, https://pubmed.ncbi.nlm.nih.gov/19543270/). It is the primary host cell receptor for Enterovirus A71 (EV-A71) and Coxsackievirus A16, the main causative agents of hand, foot, and mouth disease (HFMD) (NIH, https://pubmed.ncbi.nlm.nih.gov/19543270/; PLOS ONE, https://journals.plos.org/plosone/article?id=10.1371/journal.pone.0030507). SCARB2 facilitates viral infection by binding to the virus at the cell surface or within endosomes and triggering the pH-dependent uncoating of the viral genome (PLOS ONE, https://journals.plos.org/plosone/article?id=10.1371/journal.pmed.1004344; NIH, https://pubmed.ncbi.nlm.nih.gov/22144482/). Beyond its role as a viral receptor, SCARB2 is essential for the trafficking of the enzyme beta-glucocerebrosidase (GBA) from the endoplasmic reticulum to the lysosome; consequently, mutations in SCARB2 are linked to Action Myoclonus-Renal Failure (AMRF) syndrome and Gaucher disease (MedlinePlus, https://medlineplus.gov/genetics/gene/scarb2/; NIH, https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10130115/). Recent studies also suggest that SCARB2 promotes cancer stemness in hepatocellular carcinoma by interacting with the MYC oncogene (NIH, https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10164143/). Therapeutic strategies targeting SCARB2 include neutralizing antibodies, soluble receptor decoys, and small molecules like Polymyxin B, though care must be taken to avoid disrupting its critical physiological functions in enzyme transport (NIH, https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10164143/; NIH, https://pubmed.ncbi.nlm.nih.gov/19543270/).

Other names

LIMP-2Lysosomal integral membrane protein 2CD36L2HLGP85AMRFEPM4LIMPIISR-BII

Inhibition of viral attachment and uncoating by blocking receptor interaction; disruption of SCARB2-MYC protein-protein interaction in cancer cells.