It were revealed structural features of extracellular sialic acid-spesific lectin from saprophytic strain of Bacillus subtilis IMV B-7014 and shown this lectin constituted the complex of molecular forms (isoforms, isolectins) that obtained the working names BSL1, BSL2 and BSL3 with mM 50 kDa, 40kDa and 55 kDa respectively. They differed in physical, chemical and biological characteristics. It were investigated direct and indirect impact mechanisms of the lectin and their molecular forms. We explored the lectin showed the greatest affinity to sialic acid-containing glycoconjugates where terminal O-acetylated sialic acid associated with subterminal D-galactose via α2,3-, α2,6-or α2,8-links. Bacilli lectins completely blocked surface sialic acid-containing receptors of influenza, herpes, hepatitis C viruses and HIV and thus prevented not only their adsorption and reproduction, but also appearance and further development of viral infection. It were shown multidirectional action of the lectin isoforms on proliferation of mammalian cell cultures with different origins: normal cells (primary mouse fibroblasts), relatively normal cells (epithelioid cells, Chinese hamster ovary) and cancer cell line of HeLa. We identified an influence of gene functional condition of reparation system of bacilli cells on ability to lectin synthesis by bacteria. Using the model system RNA-polymerase of bacteriophage T7 it were established the isolectins had different effects on the yield of RNA-transcription product in vitro.

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