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Ricin B lectin-like proteins of the microsporidian Encephalitozoon cuniculi and Anncaliia algerae are involved in host-cell invasion.
Prybylski, Nastasia; Fayet, Maurine; Dubuffet, Aurore; Delbac, Frédéric; Kocer, Ayhan; Gardarin, Christine; Michaud, Philippe; El Alaoui, Hicham; Dubessay, Pascal.
Afiliação
  • Prybylski N; Université Clermont Auvergne, CNRS, Laboratoire Microorganismes: Génomes et Environnement, F-63000 Clermont-Ferrand, France; Université Clermont Auvergne, SIGMA Clermont, Institut Pascal, F-63000 Clermont-Ferrand, France. Electronic address: nastasia.prybylski@uca.fr.
  • Fayet M; Université Clermont Auvergne, CNRS, Laboratoire Microorganismes: Génomes et Environnement, F-63000 Clermont-Ferrand, France. Electronic address: maurine.fayet@uca.fr.
  • Dubuffet A; Université Clermont Auvergne, CNRS, Laboratoire Microorganismes: Génomes et Environnement, F-63000 Clermont-Ferrand, France. Electronic address: aurore.dubuffet@uca.fr.
  • Delbac F; Université Clermont Auvergne, CNRS, Laboratoire Microorganismes: Génomes et Environnement, F-63000 Clermont-Ferrand, France. Electronic address: frederic.delbac@uca.fr.
  • Kocer A; GReD, Laboratoire "Génétique, Reproduction and Développement," UMR Centre National de la Recherche Scientifique 6293, INSERM U1103, Université Clermont Auvergne, Clermont-Ferrand, France. Electronic address: ayhan.kocer@uca.fr.
  • Gardarin C; Université Clermont Auvergne, SIGMA Clermont, Institut Pascal, F-63000 Clermont-Ferrand, France. Electronic address: christine.gardarin@uca.fr.
  • Michaud P; Université Clermont Auvergne, SIGMA Clermont, Institut Pascal, F-63000 Clermont-Ferrand, France. Electronic address: philippe.michaud@uca.fr.
  • El Alaoui H; Université Clermont Auvergne, CNRS, Laboratoire Microorganismes: Génomes et Environnement, F-63000 Clermont-Ferrand, France. Electronic address: hicham.el_alaoui@uca.fr.
  • Dubessay P; Université Clermont Auvergne, SIGMA Clermont, Institut Pascal, F-63000 Clermont-Ferrand, France. Electronic address: pascal.dubessay@uca.fr.
Parasitol Int ; 87: 102518, 2022 Apr.
Article em En | MEDLINE | ID: mdl-34808329
ABSTRACT
Microsporidia are obligate intracellular pathogens capable of infecting a wide variety of hosts ranging from invertebrates to vertebrates. The infection process requires a step of prior adherence of Microsporidia to the surface of host cells. A few studies demonstrated the involvement of proteins containing a ricin-B lectin (RBL) domain in parasite infection. In this study Anncalia algerae and Encephalitozoon cuniculi genomes were screened by bioinformatic analysis to identify proteins with an extracellular prediction and possessing RBL-type carbohydrate-binding domains, being both potentially relevant factors contributing to host cell adherence. Three proteins named AaRBLL-1 and AaRBLL-2 from A. algerae and EcRBLL-1 from E. cuniculi, were selected and comparative analysis of sequences suggested their belonging to a multigenic family, with a conserved structural RBL domain despite a significant amino acid sequence divergence. The production of recombinant proteins and antibodies against the three proteins allowed their subcellular localization on the spore wall and/or the polar tube. Adherence inhibition assays based on pre-treatments with recombinant proteins or antibodies highlighted the significant decrease of the proliferation of both E. cuniculi and A. algerae, strongly suggesting that these proteins are involved in the infection process.
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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Ricina / Proteínas Fúngicas / Microsporídios / Encephalitozoon cuniculi Tipo de estudo: Prognostic_studies Limite: Animals / Humans Idioma: En Ano de publicação: 2022 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Ricina / Proteínas Fúngicas / Microsporídios / Encephalitozoon cuniculi Tipo de estudo: Prognostic_studies Limite: Animals / Humans Idioma: En Ano de publicação: 2022 Tipo de documento: Article