Revolutionizing antiviral therapy with nanobodies: Generation and prospects

Abstract

As the world continues to grapple with infectious diseases, scientists are constantly searching for effective ways to combat these deadly pathogens. One promising avenue of research is the use of nanobodies as neutralization agents. These small proteins, derived from camelid antibodies, have several unique advantages over traditional antibodies, including their small size. Nanobodies are much smaller than conventional antibodies, typically weighing in at around 15 kDa compared to the 150 kDa of a typical human antibody. This small size allows them to penetrate into tight spaces that larger molecules cannot reach, such as the crevices on the surface of viruses or bacteria. This makes them highly effective at neutralizing viruses by binding to and blocking their key functional sites. In this mini-review we discuss the construction approaches of nanobodies, and some methods to increase the half-life of nanobodies. Moreover, we discuss Nanobodies and their therapeutic potential for infectious agents.

Keywords: Antibodies; Half-life; Heavy chain; Nanobodies; VHHs.

Fig. 1

A two-step approach for generating VHH involves grafting CDRs of VH onto a VHH framework and designing a focused VHH library. The resulting weak binders lacking VL serve as templates for affinity maturation through phage display. The low association rate with the ligand is indicated by a dotted line, while dissociation is indicated by a solid line .