Human papillomavirus type 16 minor capsid protein L2 RG-1 epitope (HPV16 L2 RG-1 epitope)

The Human papillomavirus type 16 minor capsid protein L2 RG-1 epitope refers to a specific neutralizing epitope within amino acids 17-36 of the HPV16 L2 capsid protein, which becomes exposed after furin cleavage during the early stages of viral infection. This epitope is recognized by the RG-1 monoclonal antibody, which broadly neutralizes papillomaviruses by blocking L2-mediated interactions essential for virus entry. L2 itself is a minor capsid component that localizes along the inner surface of the virion beneath L1 pentamers, playing critical roles in infectious entry, including endosomal escape, cytoplasmic protrusion through the endosome membrane, and binding to cellular trafficking factors like retromer, SNX17, and COPI. The epitope's exposure post-cleavage facilitates conformational changes allowing secondary receptor uptake on basal keratinocytes, and targeting it disrupts these processes to inhibit infection. While L2 contains disordered regions whose length, rather than sequence, supports protrusion and trafficking, the RG-1 epitope is a conserved, structured motif pivotal for HPV16 infectivity. This makes it a promising antigenic target for prophylactic vaccines or therapeutics against HPV-associated diseases like cervical cancer.

Other names

HPV16 L2 RG1 epitopeL2 neutralizing epitope (aa17-36)RG-1 monoclonal antibody epitope

Neutralization of virus entry by binding to exposed epitope post-furin cleavage, preventing secondary receptor interaction and infection