Identification of the Autochaperone Domain in the Type Va Secretion System (T5aSS): Prevalent Feature of Autotransporters with a β-Helical Passenger

Autor: Maricarmen Rojas-Lopez, Mohamed A. Zorgani, Lawrence A. Kelley, Xavier Bailly, Andrey V. Kajava, Ian R. Henderson, Fabio Polticelli, Mariagrazia Pizza, Roberto Rosini, Mickaël Desvaux
Přispěvatelé: Microbiologie Environnement Digestif Santé - Clermont Auvergne (MEDIS), INRA Clermont-Ferrand-Theix-Université Clermont Auvergne (UCA), Laboratoire des symbioses tropicales et méditerranéennes (UMR LSTM), Centre de Coopération Internationale en Recherche Agronomique pour le Développement (Cirad)-Université Montpellier 1 (UM1)-Institut de Recherche pour le Développement (IRD)-Institut National de la Recherche Agronomique (INRA)-Université Montpellier 2 - Sciences et Techniques (UM2)-Université de Montpellier (UM)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro), INRA, UR346 Epidémiologie Animale, Institut National de la Recherche Agronomique (INRA), Centre de recherche en Biologie Cellulaire (CRBM), Université Montpellier 2 - Sciences et Techniques (UM2)-Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM)-Université Montpellier 1 (UM1), Institute of Microbiology and Infection, University of Birmingham [Birmingham], Dipartimento di Biologia, Roma Tre University, GlaxoSmithKline [Siena, Italy] (GSK), Microbiologie Environnement Digestif Santé (MEDIS), Institut National de la Recherche Agronomique (INRA)-Université Clermont Auvergne [2017-2020] (UCA [2017-2020]), Structural Bioinformatics Group, Imperial College London, Unité Mixte de Recherche d'Épidémiologie des maladies Animales et zoonotiques (UMR EPIA), Institut National de la Recherche Agronomique (INRA)-VetAgro Sup - Institut national d'enseignement supérieur et de recherche en alimentation, santé animale, sciences agronomiques et de l'environnement (VAS), Centre de recherche en Biologie cellulaire de Montpellier (CRBM), Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS), Università degli Studi Roma Tre = Roma Tre University (ROMA TRE), INRA Clermont-Ferrand-Theix-Université Clermont Auvergne [2017-2020] (UCA [2017-2020]), Université Clermont Auvergne (UCA)-INRA Clermont-Ferrand-Theix, Université Montpellier 1 (UM1)-Institut de Recherche pour le Développement (IRD)-Institut National de la Recherche Agronomique (INRA)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro), Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Université de Montpellier (UM)-Centre de Coopération Internationale en Recherche Agronomique pour le Développement (Cirad)-Université Montpellier 2 - Sciences et Techniques (UM2), Rojas-Lopez, Maricarmen, Zorgani, Mohamed A., Kelley, Lawrence A., Bailly, Xavier, Kajava, Andrey V., Henderson, Ian R., Polticelli, Fabio, Pizza, Mariagrazia, Rosini, Roberto, Desvaux, Mickaël, Université Montpellier 1 (UM1)-Université Montpellier 2 - Sciences et Techniques (UM2)-Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS)
Jazyk: angličtina
Rok vydání: 2018
Předmět:
0301 basic medicine
Microbiology (medical)
autochaperone domain
Sequence analysis
Structural alignment
lcsh:QR1-502
translocation
Virulence
protein secretion system
autotransporters
Type V secretion system
outer membrane protein
protein translocation
diderm-LPS Gram-negative bacteria
Computational biology
Biology
Outer membrane proteins
Microbiology
lcsh:Microbiology
03 medical and health sciences
Hydrolase
Secretion
ComputingMilieux_MISCELLANEOUS
Original Research
Protein translocation
030102 biochemistry & molecular biology
sécrétion protéique
Autochaperone domain
[SDV.BIBS]Life Sciences [q-bio]/Quantitative Methods [q-bio.QM]
030104 developmental biology
Secretory protein
Autotransporter
Diderm-LPS Gram-negative bacteria
Outer membrane protein
Protein secretion system
Bacterial outer membrane
protéine de la membrane externe
Autotransporters
Zdroj: Frontiers in Microbiology
Frontiers in Microbiology, Frontiers Media, 2018, 8, ⟨10.3389/fmicb.2017.02607⟩
Frontiers in Microbiology, 2018, 8, ⟨10.3389/fmicb.2017.02607⟩
Frontiers in Microbiology, Vol 8 (2018)
Frontiers in Microbiology (8), . (2018)
ISSN: 1664-302X
DOI: 10.3389/fmicb.2017.02607⟩
Popis: International audience; Autotransporters (ATs) belong to a family of modular proteins secreted by the Type V, subtype a, secretion system (T5aSS) and considered as an important source of virulence factors in lipopolysaccharidic diderm bacteria (archetypical Gram-negative bacteria). While exported by the Sec pathway, the ATs are further secreted across the outer membrane via their own C-terminal translocator forming a b-barrel, through which the rest of the protein, namely the passenger, can pass. In several ATs, an autochaperone domain (AC) present at the C-terminal region of the passenger and upstream of the translocator was demonstrated as strictly required for proper secretion and folding. However, considering it was functionally characterised and identified only in a handful of ATs, wariness recently fells on the commonality and conservation of this structural element in the T5aSS. To circumvent the issue of sequence divergence and taking advantage of the resolved three-dimensional structure of some ACs, identification of this domain was performed following structural alignment among all AT passengers experimentally resolved by crystallography before searching in a dataset of 1523 ATs. While demonstrating that the AC is indeed a conserved structure found in numerous ATs, phylogenetic analysis further revealed a distribution into deeply rooted branches, from which emerge 20 main clusters. Sequence analysis revealed that an AC could be identified in the large majority of SAATs (self-associating ATs) but not in any LEATs (lipase/esterase ATs) nor in some PATs (protease autotransporters) and PHATs (phosphatase/hydrolase ATs). Structural analysis indicated that an AC was present in passengers exhibiting single-stranded right-handed parallel b-helix, whatever the type of b-solenoid, but not with a-helical globular fold. From this investigation, the AC of type 1 appears as a prevalent and conserved structural element exclusively associated to b-helical AT passenger and should promote further studies about the protein secretion and folding via the T5aSS, especially toward a-helical AT passengers.
Databáze: OpenAIRE
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