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Open AccessArticle

A Monoclonal Antibody against the C-Terminal Domain of Bacillus cereus Hemolysin II Inhibits HlyII Cytolytic Activity

1
Pushchino Branch, Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 6 Prospekt Nauki, 142290 Pushchino, Moscow Region, Russia
2
FSBIS FRC Pushchino Scientific Centre of Biological Research, G.K. Skryabin Institute of Biochemistry and Physiology of Microorganisms, Russian Academy of Sciences, 5 Prospekt Nauki, 142290 Pushchino, Moscow Region, Russia
3
Pushchino State Institute of Natural Sciences, 3 Prospekt Nauki, 142290 Pushchino, Moscow Region, Russia
4
Protein Institute of the Russian Academy of Sciences, 4 Prospekt Nauki, 142290 Pushchino, Moscow Region, Russia
*
Author to whom correspondence should be addressed.
Toxins 2020, 12(12), 806; https://doi.org/10.3390/toxins12120806
Received: 30 October 2020 / Revised: 19 November 2020 / Accepted: 16 December 2020 / Published: 19 December 2020
(This article belongs to the Special Issue Antibodies for Toxins: From Detection to Therapeutics)
Bacillus cereus is the fourth most common cause of foodborne illnesses that produces a variety of pore-forming proteins as the main pathogenic factors. B. cereus hemolysin II (HlyII), belonging to pore-forming β-barrel toxins, has a C-terminal extension of 94 amino acid residues designated as HlyIICTD. An analysis of a panel of monoclonal antibodies to the recombinant HlyIICTD protein revealed the ability of the antibody HlyIIC-20 to inhibit HlyII hemolysis. A conformational epitope recognized by HlyIIC-20 was found. by the method of peptide phage display and found that it is localized in the N-terminal part of HlyIICTD. The HlyIIC-20 interacted with a monomeric form of HlyII, thus suppressing maturation of the HlyII toxin. Protection efficiencies of various B. cereus strains against HlyII were different and depended on the epitope amino acid composition, as well as, insignificantly, on downstream amino acids. Substitution of L324P and P324L in the hemolysins ATCC14579T and B771, respectively, determined the role of leucine localized to the epitope in suppressing the hemolysis by the antibody. Pre-incubation of HlyIIC-20 with HlyII prevented the death of mice up to an equimolar ratio. A strategy of detecting and neutralizing the toxic activity of HlyII could provide a tool for monitoring and reducing B. cereus pathogenicity. View Full-Text
Keywords: pore-forming toxin; hybridoma; bacteriophage display; epitope mapping; neutralizing monoclonal antibody; oligomerization; ELISA; hemolysis; in vivo efficiency pore-forming toxin; hybridoma; bacteriophage display; epitope mapping; neutralizing monoclonal antibody; oligomerization; ELISA; hemolysis; in vivo efficiency
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MDPI and ACS Style

Rudenko, N.; Nagel, A.; Zamyatina, A.; Karatovskaya, A.; Salyamov, V.; Andreeva-Kovalevskaya, Z.; Siunov, A.; Kolesnikov, A.; Shepelyakovskaya, A.; Boziev, K.; Melnik, B.; Brovko, F.; Solonin, A. A Monoclonal Antibody against the C-Terminal Domain of Bacillus cereus Hemolysin II Inhibits HlyII Cytolytic Activity. Toxins 2020, 12, 806. https://doi.org/10.3390/toxins12120806

AMA Style

Rudenko N, Nagel A, Zamyatina A, Karatovskaya A, Salyamov V, Andreeva-Kovalevskaya Z, Siunov A, Kolesnikov A, Shepelyakovskaya A, Boziev K, Melnik B, Brovko F, Solonin A. A Monoclonal Antibody against the C-Terminal Domain of Bacillus cereus Hemolysin II Inhibits HlyII Cytolytic Activity. Toxins. 2020; 12(12):806. https://doi.org/10.3390/toxins12120806

Chicago/Turabian Style

Rudenko, Natalia; Nagel, Alexey; Zamyatina, Anna; Karatovskaya, Anna; Salyamov, Vadim; Andreeva-Kovalevskaya, Zhanna; Siunov, Alexander; Kolesnikov, Alexander; Shepelyakovskaya, Anna; Boziev, Khanafiy; Melnik, Bogdan; Brovko, Fedor; Solonin, Alexander. 2020. "A Monoclonal Antibody against the C-Terminal Domain of Bacillus cereus Hemolysin II Inhibits HlyII Cytolytic Activity" Toxins 12, no. 12: 806. https://doi.org/10.3390/toxins12120806

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