Sequence analysis and confirmation of the type IV pili-associated proteins PilY1, PilW and PilV in Acidithiobacillus thiooxidans

Acidithiobacillus thiooxidans is an acidophilic chemolithoautotrophic bacterium widely used in the mining industry due to its metabolic sulfur-oxidizing capability. The biooxidation of sulfide minerals is enhanced through the attachment of At. thiooxidans cells to the mineral surface. The Type IV pi...

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Bibliographic Details
Published in:PloS one 2019-01, Vol.14 (1), p.e0199854-e0199854
Main Authors: Alfaro-Saldaña, Elvia, Hernández-Sánchez, Araceli, Patrón-Soberano, O Araceli, Astello-García, Marizel, Méndez-Cabañas, J Alfredo, García-Meza, J Viridiana
Format: Article
Language:English
Subjects:
Acid mine drainage
Acidithiobacillus thiooxidans - genetics
Aerobic bacteria
Analysis
Assembly
Attachment
Bacteria
Biofilms
Biology and Life Sciences
Biosynthesis
Cladistic analysis
Colonization
Computer and Information Sciences
Domains
Energy transduction
Evolution
Fimbriae Proteins - genetics
Fimbriae, Bacterial - genetics
Functionals
Genomes
Homology
Iron
Medicine and Health Sciences
Microorganisms
Mine tailings
Minerals
Mining
Mining industry
Motility
mRNA
Neisseria - genetics
Oxidation
Phylogeny
Pili
Prokaryotes
Protein Domains
Proteins
Pseudomonas aeruginosa - genetics
Research and Analysis Methods
Sequence Analysis, DNA
Signal transduction
Sulfide
Sulfur
Three dimensional models
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Summary:Acidithiobacillus thiooxidans is an acidophilic chemolithoautotrophic bacterium widely used in the mining industry due to its metabolic sulfur-oxidizing capability. The biooxidation of sulfide minerals is enhanced through the attachment of At. thiooxidans cells to the mineral surface. The Type IV pili (TfP) of At. thiooxidans may play an important role in the bacteria attachment since TfP play a key adhesive role in the attachment and colonization of different surfaces. In this work, we report for the first time the mRNA sequence of three TfP proteins from At. thiooxidans, the adhesin protein PilY1 and the TfP pilins PilW and PilV. The nucleotide sequences of these TfP proteins show changes in some nucleotide positions with respect to the corresponding annotated sequences. The bioinformatic analyses and 3D-modeling of protein structures sustain their classification as TfP proteins, as structural homologs of the corresponding proteins of Ps. aeruginosa, results that sustain the role of PilY1, PilW and PilV in pili assembly. Also, that PilY1 comprises the conserved Neisseria-PilC (superfamily) domain of the tip-associated adhesin, while PilW of the superfamily of putative TfP assembly proteins and PilV belongs to the superfamily of TfP assembly protein. In addition, the analyses suggested the presence of specific functional domains involved in adhesion, energy transduction and signaling functions. The phylogenetic analysis indicated that the PilY1 of Acidithiobacillus genus forms a cohesive group linked with iron- and/or sulfur-oxidizing microorganisms from acid mine drainage or mine tailings.
ISSN:1932-6203
1932-6203
DOI:10.1371/journal.pone.0199854