Engineering Lactobacillus rhamnosus GG and GR-1 to express HIV-inhibiting griffithsin

With human immunodeficiency virus (HIV) infections being one of the top infectious diseases worldwide, the interest in carbohydrate-binding agents (CBAs) as therapeutic agents that can block HIV is growing [1]. Two promising peptidic CBAs, with documented activity against HIV and so far unknown side-effects for human host cells, are actinohivin (AH) and griffithsin (GRFT) [2, 3]. AH is a 12.5 kDa lectin isolated from the actinomycete Longisporum albida [4, 5]. AH consists of 114 amino acid residues, divided into three segments, forming three sugar-binding pockets to accommodate Man- α(1-2)-Man residues of N-linked glycans present on the surface of the HIV envelope glycoprotein gp120, therefore inhibiting HIV infection [3, 5, 6].

Source: International Journal of Antimicrobial Agents - July 21, 2018 Category: Drugs & Pharmacology Authors: Mariya I. Petrova, Marianne F.L. van den Broek, Irina Spacova, Tine L.A. Verhoeven, Jan Balzarini, Jos Vanderleyden, Dominique Schols, Sarah Lebeer Source Type: research