| Title | Gallibacterium elongation factor-Tu possesses amyloid-like protein characteristics, participates in cell adhesion, and is present in biofilms |
|---|---|
| Author | Jaqueline López-Ochoa1, J. Fernando Montes-García2, Candelario Vázquez1, Patricia Sánchez-Alonso1, Victor M. Pérez-Márquez3, Patrick J. Blackall4, Sergio Vaca2, and Erasmo Negrete-Abascal2* |
| Address | 1Centro de Investigaciones en Ciencias Microbiológicas, Benemérita Universidad Autónoma de Puebla, Puebla 72560, Mexico, 2Carrera de Biología, Facultad de Estudios Superiores Iztacala, Universidad Nacional Autónoma de México, Tlalnepantla, Estado de México 54090, Mexico, 3Biotecnología Veterinaria de Puebla, Tehuacán, Puebla, 75760, Mexico, 4Queensland Alliance for Agriculture and Food Innovation, The University of Queensland, St Lucia 4067, Queensland, Australia |
| Bibliography | Journal of Microbiology, 55(9),745–752, 2017, |
| DOI | 10.1007/s12275-017-7077-0 |
| Key Words | Gallibacterium, amyloid proteins, curli fimbria, Congo red binding, adhesin |
| Abstract | Gallibacterium, which is a bacterial pathogen in chickens, can form biofilms. Amyloid proteins present in biofilms bind Congo red dye. The aim of this study was to characterize the cell-surface amyloid-like protein expressed in biofilms formed by Gallibacterium strains and determine the relationship between this protein and curli, which is an amyloid protein that is commonly expressed by members of the Enterobacteriaceae family. The presence of amyloid-like proteins in outer membrane protein samples from three strains of G. anatis and one strain of Gallibacterium genomospecies 2 was evaluated. A protein identified as elongation factor-Tu (EF-Tu) by mass spectrometric analysis and in silico analysis was obtained from the G. anatis strain F149T. This protein bound Congo red dye, cross-reacted with anti-curli polyclonal serum, exhibited polymerizing properties and was present in biofilms. This protein also reacted with pooled serum from chickens that were experimentally infected with G. anatis, indicating the in vivo immunogenicity of this protein. The recombinant EF-Tu purified protein, which was prepared from G. anatis 12656-12, polymerizes under in vitro conditions, forms filaments and interacts with fibronectin and fibrinogen, all of which suggest that this protein functions as an adhesin. In summary, EF-Tu from G. anatis presents amyloid characteristics, is present in biofilms and could be relevant for the pathogenesis of G. anatis. |