PubMed_ArguminSci  

PubMed:28865072 JSONTXT 6 Projects

Annnotations TAB TSV DIC JSON TextAE

Id Subject Object Predicate Lexical cue
T1 143-220 DRI_Background denotes Gallibacterium, which is a bacterial pathogen in chickens, can form biofilms.
T2 221-277 DRI_Background denotes Amyloid proteins present in biofilms bind Congo red dye.
T3 278-575 DRI_Background denotes 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.
T4 576-697 DRI_Background denotes The presence of amyloid-like proteins in outer membrane protein samples from three strains of G. anatis and one strain of
T5 727-743 DRI_Background denotes 2 was evaluated.
T6 744-896 DRI_Background denotes 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.
T7 897-1041 DRI_Outcome denotes This protein bound Congo red dye, cross-reacted with anti-curli polyclonal serum, exhibited polymerizing properties and was present in biofilms.
T8 1042-1204 DRI_Outcome denotes This protein also reacted with pooled serum from chickens that were experimentally infected with G. anatis, indicating the in vivo immunogenicity of this protein.
T9 1205-1454 DRI_Background denotes 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.