microbeПроблемы особо опасных инфекцийProblems of Particularly Dangerous Infections0370-10692658-719XRussian Research Anti-Plague Institute “Microbe”10.21055/0370-1069-2014-3-52-56microbe-163Research ArticleМИКРОБИОЛОГИЯMICROBIOLOGYМембранный белок OmpT холерного вибриона как возможный представитель омптинов семейства VibrionaceaeCholera Vibrio Membrane Protein OmpT as an Omptin Belonging to Vibrionaceae FamilyМишанькинБ. Н.Mishan’KinB. N.plague@aaanet.ruДувановаО. В.DuvanovaO. V.plague@aaanet.ruРомановаЛ. В.RomanovaL. V.plague@aaanet.ruШипкоЕ. С.ShipkoE. S.plague@aaanet.ruВодопьяновА. С.Vodop’YanovA. S.plague@aaanet.ruРостовский-на-Дону научно-исследовательский противочумный институтРоссияRostov-on-Don Research Anti-Plague InstituteRussian Federation201420092014035256Copyright © Мишанькин Б.Н., Дуванова О.В., Романова Л.В., Шипко Е.С., Водопьянов А.С., 20142014Мишанькин Б.Н., Дуванова О.В., Романова Л.В., Шипко Е.С., Водопьянов А.С.Mishan’Kin B.N., Duvanova O.V., Romanova L.V., Shipko E.S., Vodop’Yanov A.S.This work is licensed under a Creative Commons Attribution 4.0 License.https://journal.microbe.ru/jour/article/view/163

В работе рассматривается состояние проблемы омптинов энтеробактерий, их структура и функции, а также возможная роль в патогенезе вызываемых ими инфекций. У холерного вибриона выделен и очищен с помощью дифференциального центрифугирования и колоночной хроматографии пориновый белок наружных мембран OmpT c молекулярной массой около 40 кДа, синтез которого находится под контролем сложной системы регуляции. Он не содержит в своем составе цистеина, наделен протеолитической активностью с широкой субстратной специфичностью: способен гидролизовать фибрин, протамин, желатин, активировать плазминоген человека в плазмин, что обеспечивает известные преимущества вибрионам во время пребывания в кишечнике чувствительного хозяина. Сравнительный компьютерный анализ аминокислотной последовательности показал, что белок OmpT холерного вибриона лишь отдаленно родственен омптинам энтеробактерий (13 % идентичности и сходства) и возможно принадлежит к новому классу поринов семейства Vibrionaceae .

Concerned are the issues related to enterobacteria omptins, their structure and functionality, as well as alternative role in pathogenesis of the infections induced by them. Isolated from cholera vibrio, and later purified using differential centrifugation and column chromatography has been porin protein of the OmpT outer membranes, with the molar mass of approximately 40 kDa. Synthesis of porin is under control of the complex regulatory system. It does not contain cysteine, but possesses proteolytic activity with broad substrate specificity: it hydrolyzes fibrin, protamin, gelatine; transduces human plasminogen into plasmin, which provides for the well-known advantages for the vibrios in the intestine of a susceptible host. Comparative computer-assisted analysis of amino acid sequence has revealed that cholera vibrio OmpT protein relates to the omptins of enterobacteria as a far-remotely one, and has 13 % identity and similarity to it. OmpT protein is probably affiliated to a new class of porins of the family Vibrionaceae .

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The authors declare that there are no conflicts of interest present.