La deficiencia en el transporte de N-acetilglucosamina en Lysinibacillus sphaericus ASB13052 afecta el proceso de esporulación e incrementa la actividad hemolítica de su S-layer

Lysinibacillus sphaericus is a bacterium that, along with Bacillus thuringiensis var. israelensis, is considered the best biological insecticide for controlling mosquito larvae and an eco-friendly alternative to chemical insecticides. It depends on peptidic molecules such as N-acetylglucosamine to obtain carbon sources and possesses a phosphotransferase system (PTS) for their incorporation. Some strains carry S-layer proteins, whose involvement in metal retention and larvicidal activity against disease-carrying mosquitoes has been demonstrated. Alterations in the amino sugar incorporation system could affect the protein profile and functionality. Strain ASB13052 and the isogenic mutant in the ptsH gene, which is predominant in the PTS signaling pathway, were used in this study. For the first time, the presence of N-glycosylated S-layer proteins was confirmed in both strains, with a variation in their molecular weight pattern depending on the growth phase. In the exponential phase, an S-layer protein greater than 130 kDa was found in the ptsH mutant, which was absent in the wild-type strain. The mutant strain exhibited altered and incomplete low quality sporulation processes. Hemolysis analysis, associated with larvicidal activity, showed that the ptsH mutant has higher lytic efficiency, correlating with the high molecular weight protein. The results allow us to propose the potential effects that arise as a result of the absence of amino sugar transport on hemolytic activity, S-layer isoforms, and the role of N-acetylglucosamine in larvicidal activity.