Identification of two adhesins of Actinobacillus seminis

Montes-García, J. Fernando; Martinez, Delil A. Chincoya; Pacheco, Sergio Vaca; Cruz, Candelario Vázquez; Alonso, Patricia Sánchez; Xicohtencatl‐Cortes, Juan; Trujillo-Ruíz, H. H.; Negrete-Abascal, Erasmo

doi:10.1016/j.smallrumres.2018.08.013

Cited by 6 publications

(2 citation statements)

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“…It has been reported that the EF-Tu of many bacterial species is involved in adhesion to human epithelial cells and to extracellular matrix proteins [ 15 , 16 , 17 , 18 , 19 , 20 , 21 , 22 , 23 ]. E. coli has two copies of the tuf gene ( tufA and tufB ), which are almost identical but located in different chromosomal regions, allowing the deletion of one copy without loss of cell viability [ 51 ].…”

Section: Resultsmentioning

confidence: 99%

“…In addition, it has been demonstrated that this protein may also localize on the surface of some bacteria, where it may play a role in colonization-associated phenotypes or even in virulence [ 4 , 5 ]. Depending on the microorganism, EF-Tu may act as an adhesin with binding capabilities to host proteins, including fibrinogen [ 15 , 16 , 17 ], fibronectin [ 17 , 18 , 19 , 20 , 21 , 22 , 23 ], laminin [ 23 ], plasminogen [ 15 , 16 , 24 ], fetuin [ 25 ], factor H [ 15 , 16 , 24 , 26 ] and mucin [ 27 , 28 , 29 ]. A recent study showed the localization of EF-Tu on the bacterial surface of some uropathogenic E. coli (UPEC) strains and suggested that this protein could promote kidney stone formation [ 30 ].…”

Section: Introductionmentioning

confidence: 99%

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Deciphering Additional Roles for the EF-Tu, l-Asparaginase II and OmpT Proteins of Shiga Toxin-Producing Escherichia coli

et al. 2020

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Shiga toxin-producing Escherichia coli (STEC) causes outbreaks and sporadic cases of gastroenteritis. STEC O157:H7 is the most clinically relevant serotype in the world. The major virulence determinants of STEC O157:H7 are the Shiga toxins and the locus of enterocyte effacement. However, several accessory virulence factors, mainly outer membrane proteins (OMPs) that interact with the host cells may contribute to the virulence of this pathogen. Previously, the elongation factor thermo unstable (EF-Tu), l-asparaginase II and OmpT proteins were identified as antigens in OMP extracts of STEC. The known subcellular location of EF-Tu and l-asparaginase II are the cytoplasm and periplasm, respectively. Therefore, we investigate whether these two proteins may localize on the surface of STEC and, if so, what roles they have at this site. On the other hand, the OmpT protein, a well characterized protease, has been described as participating in the adhesion of extraintestinal pathogenic E. coli strains. Thus, we investigate whether OmpT has this role in STEC. Our results show that the EF-Tu and l-asparaginase II are secreted by O157:H7 and may also localize on the surface of this bacterium. EF-Tu was identified in outer membrane vesicles (OMVs), suggesting it as a possible export mechanism for this protein. Notably, we found that l-asparaginase II secreted by O157:H7 inhibits T-lymphocyte proliferation, but the role of EF-Tu at the surface of this bacterium remains to be elucidated. In the case of OmpT, we show its participation in the adhesion of O157:H7 to human epithelial cells. Thus, this study extends the knowledge of the pathogenic mechanisms of STEC.

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Deciphering Additional Roles for the EF-Tu, l-Asparaginase II and OmpT Proteins of Shiga Toxin-Producing Escherichia coli

et al. 2020

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Actinobacillus seminis GroEL-homologous protein agglutinates sheep erythrocytes

Montes-García

Delgado-Tapia

Vázquez-Cruz

et al. 2019

Antonie van Leeuwenhoek

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Characterization of Actinobacillus seminis biofilm formation

Rojas¹,

Zenteno

Cruz

et al. 2020

Antonie van Leeuwenhoek

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Actinobacillus seminis is an autochthonous gram-negative bacterium that affects reproductive organs, causing epididymitis, low fertility, and occasional abortions in ovine and goats. The virulence factors and the pathogenicity mechanisms of A. seminis have not been clearly elucidated yet. In this work, biofilm production by A. seminis in in vitro assays is described and characterized. After 48-h incubation at 37 °C in trypticase soy broth, A. seminis formed biofilms containing an extracellular matrix comprised mainly of fibrillar material. Microaerophilia or the presence of calcium diminished biofilm formation in approximately 50% and 70%, respectively, but low iron concentrations increased it 40%. Through enzymatic digestion, it was found that

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Identification of two adhesins of Actinobacillus seminis

Cited by 6 publications

References 23 publications

Deciphering Additional Roles for the EF-Tu, l-Asparaginase II and OmpT Proteins of Shiga Toxin-Producing Escherichia coli

Deciphering Additional Roles for the EF-Tu, l-Asparaginase II and OmpT Proteins of Shiga Toxin-Producing Escherichia coli

Actinobacillus seminis GroEL-homologous protein agglutinates sheep erythrocytes

Characterization of Actinobacillus seminis biofilm formation

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