Specific Interaction of NovelFriunavirusPhages Encoding Tailspike Depolymerases with Corresponding Acinetobacter baumannii Capsular Types

Specific Interaction of NovelFriunavirusPhages Encoding Tailspike Depolymerases with Corresponding Acinetobacter baumannii Capsular Types Full article

Journal

Journal of Virology
ISSN: 1098-5514 , E-ISSN: 1070-6321

Output data

Year: 2021, Volume: 95, Number: 5, Article number : e01714-20, Pages count : DOI: 10.1128/jvi.01714-20

Authors

Popova A.V. ^1,2,3 , Shneider M.M. ^1,4 , Arbatsky N.P. ⁵ , Kasimova A.A. ⁵ , Senchenkova S.N. ⁵ , Shashkov A.S. ⁵ , Dmitrenok A.S. ⁵ , Chizhov A.O. ⁵ , Mikhailova Y.V. ⁶ , Shagin D.A. ⁷ , Sokolova O.S. ⁸ , Timoshina O.Y. ^6,4 , Kozlov R.S. ¹ , Miroshnikov K.A. ⁴ , Knirel Y.A. ⁵

Affiliations

1	Institute of Antimicrobial Chemotherapy, Smolensk State Medical University, Smolensk, Russia
2	Moscow Institute of Physics and Technology (National Research University), Dolgoprudny, Moscow Region, Russia
3	State Research Center for Applied Microbiology and Biotechnology, Obolensk, Moscow Region, Russia
4	Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, Russia
5	Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, Moscow, Russia
6	Central Scientific Research Institute of Epidemiology, Moscow, Russia
7	Pirogov Russian National Research Medical University, Moscow, Russia
8	Lomonosov Moscow State University, Moscow, Russia

Acinetobacter baumannii is one of the most clinically important nosocomial pathogens. The World Health Organization refers it to its “critical priority” category to develop new strategies for effective therapy. This microorganism is capable of producing structurally diverse capsular polysaccharides (CPSs), which serve as primary receptors for A. baumannii bacteriophages carrying polysaccharide-degrading enzymes. In this study, eight novel bacterial viruses that specifically infect A. baumannii strains belonging to K2/K93, K32, K37, K44, K48, K87, K89, and K116 capsular types were isolated and characterized. The overall genomic architecture demonstrated that these viruses are representatives of the Friunavirus genus of the family Autographiviridae. The linear double-stranded DNA phage genomes of 41,105 to 42,402 bp share high nucleotide sequence identity, except for genes encoding structural depolymerases or tailspikes, which determine the host specificity. Deletion mutants lacking N-terminal domains of tailspike proteins were cloned, expressed, and purified. The structurally defined CPSs of the phage bacterial hosts were cleaved with the specific recombinant depolymerases, and the resultant oligosaccharides that corresponded to monomers or/and dimers of the CPS repeats (K units) were isolated. Structures of the derived oligosaccharides were established by nuclear magnetic resonance spectroscopy and high-resolution electrospray ionization mass spectrometry. The data obtained showed that all depolymerases studied were glycosidases that specifically cleave the A. baumannii CPSs by the hydrolytic mechanism, in most cases, by the linkage between the K units.

Popova A.V. , Shneider M.M. , Arbatsky N.P. , Kasimova A.A. , Senchenkova S.N. , Shashkov A.S. , Dmitrenok A.S. , Chizhov A.O. , Mikhailova Y.V. , Shagin D.A. , Sokolova O.S. , Timoshina O.Y. , Kozlov R.S. , Miroshnikov K.A. , Knirel Y.A.
Specific Interaction of NovelFriunavirusPhages Encoding Tailspike Depolymerases with Corresponding Acinetobacter baumannii Capsular Types
Journal of Virology. 2021. V.95. N5. e01714-20 . DOI: 10.1128/jvi.01714-20 WOS OpenAlex

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