Identification of a Hemagglutinin from Gallibacterium anatis

Montes-García, J. Fernando; Vaca, Sergio; Vázquez-Cruz, Candelario; Soriano‐Vargas, Edgardo; Aguilar-Romero, Francisco; Blackall, P. J.; Negrete-Abascal, Erasmo

doi:10.1007/s00284-015-0969-5

Cited by 9 publications

(7 citation statements)

References 22 publications

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“…In contrast, the putative hemoglobin-binding protein (70-kDa protein from the culture without the added chelating agent) was at a higher concentration in samples from the F149 T strain, and a tiny band was observed in iron-restricted conditions ( Figure 4 ). G. anatis F149 T is a non-hemolytic and non-virulent strain with few studies on its participation in gallibacteriosis ( Montes-García et al, 2016 ; Zhang et al, 2017 ). However, this G. anatis strain also expresses different virulence factors as virulent strains do, but in a lower amount.…”

Section: Discussionmentioning

confidence: 99%

“…E. coli and Pseudomonas aeruginosa PAO1 were cultured in LB-broth to test siderophores production. G. anatis F114 and ESV34 strains hemolytic varieties ( Montes-García et al, 2016 ) were also included in this study. Several fur -mutant strains were obtained in this work, but the mutant assayed in vivo here was Ω fur 126.13.…”

Section: Methodsmentioning

confidence: 99%

“…Few virulence factors have been described to be expressed by this bacterium: chicken IgG-degrading secreted proteases ( García-Gómez et al, 2005 ), expression of a RTX (Repeat in toxin) protein ( Kristensen et al, 2010 ), as well as the ability to agglutinate red blood cells ( Zepeda et al, 2009 ; Montes-García et al, 2016 ), and the ability to adhere to plastic surfaces and to form biofilms on glass ( Vaca et al, 2011 ; Persson and Bojesen, 2015 ). This last capability could be supported by the fimbriae expression described recently ( Salgado-Lucio et al, 2012 ; Bager et al, 2013 ; Kudirkiene et al, 2014 ; López-Ochoa et al, 2017 ) or by the participation of other molecules as putative adhesins like the EF-Tu protein ( López-Ochoa et al, 2017 ).…”

Section: Introductionmentioning

confidence: 99%

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A putative siderophore receptor of Gallibacterium anatis 12656-12 under Fur control also binds hemoglobin

et al. 2022

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Pasteurellaceae family members obtain iron directly from host proteins or through siderophore-dependent mechanisms. Although Gallibacterum anatis expresses different virulence factors, its response to growth under iron restriction is unknown. G. anatis cultured in the presence of 2,2′-dipyridyl, up-expressed an approximately 65 kDa protein and repressed the expression of a 70 kDa protein. MALDI-TOF analysis of those proteins indicated homology with CirA (65 kDa), a protein involved in iron-siderophore acquisition in Mannheimia succinoproducens and a TonB-dependent receptor (70 kDa protein), a protein that binds chicken hemoglobin; however, G. anatis siderophore production was not detected by chromo azurol S (CAS)-BHI agar determination. This putative G. anatis siderophore receptor is under Fur control, but not the hemoglobin binding protein, as observed in G. anatis 12656-12 fur mutant (Ω fur 126.13) grown in the presence or not of 2,2′-dipyridyl. The addition of FeCl3 to the culture medium diminished the growth and biofilm production in approximately 30% and 35%, respectively, in the wild-type strain, but the growth of Ω fur 126.13 strain was not affected and biofilm production increased in 35%. G. anatis Ω fur 126.13 presented lower virulence when it was inoculated to 35-day-old chickens in comparison to the wild-type strain. The induction of more than one iron uptake mechanism could benefit pathogenic microorganisms such as Gallibacterium.

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Section: Discussionmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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A putative siderophore receptor of Gallibacterium anatis 12656-12 under Fur control also binds hemoglobin

et al. 2022

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“…Different anti-sera against different proteins were used to determine their potential participation in biofilm formation: phosphoglycerate mutase (PGM), a protein functioning as afimbrial adhesin in A. seminis (Montes Garcı ´a et al 2018a); elongation factor Tu (EF-Tu) or hemagglutinin, both proteins previously described in Gallibacterium anatis biofilms (Montes Garcı ´a et al 2016;Lo ´pez-Ochoa et al 2017); OMP2-like from Mannheimia haemolytica; an amyloid-like protein found in M. haemolytica biofilm (Montes Garcı ´a et al 2018b); A. seminis biofilm matrix and sera from sheep with epididymitis. An overnight A. seminis culture was adjusted to 1.0 OD 600 nm, mixed with each antiserum (1:10), and incubated for 1 h under agitation.…”

Section: Effect Of Different Anti-sera On Biofilm Formationmentioning

confidence: 99%

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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“…Many of these FHA-like proteins act as adhesins, similar to FHA of B. pertussis, and some have been implicated in biofilm and aggregative growth, a precursor to biofilm (300,(357)(358)(359)(360)(361)(362)(363)(364).…”

Section: Introductionmentioning

confidence: 99%

The "Mystery Phases": Bordetella Adenylate Cyclase Toxin and biofilm in the Bvg-Intermediate Phase & Bordetella pertussis Motility and Flagella in the Bvg-Minus Phase

Hoffman¹

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Bordetella pertussis is the Gram-negative bacterial pathogen responsible for the life-threatening disease, whooping cough (pertussis). The bacterium has been of increasing interest in the research community due to the reemergence of this vaccine-preventable disease. In fact, the numbers of pertussis cases reported to the CDC annually are similar to those reported prior to the introduction of the whole cell pertussis vaccine. The increased number of cases coincides with the transition to the acellular vaccine, comprised of just one to five B. pertussis antigens (pertussis toxin, filamentous hemagglutinin, pertactin, fimbriae 2 and fimbriae 3). This correlation, while not the only contributing factor to reemergence of the disease, highlights the fact that not enough was known about the biology of B. pertussis before the acellular vaccine was created. In fact, it has only recently been shown that B. pertussis forms biofilm during infection, and that biofilm may be a virulence trait of Bordetella. These biofilms form both in vitro on abiotic surfaces and in vivo in the mouse trachea and nasopharynx.Biofilms are defined as surface-associated bacterial growth, in which the bacteria are covered in extracellular polymeric substance (EPS or matrix), comprised of polysaccharides, eDNA, and proteins. These microbial communities are often associated with persistent infections and in some cases, asymptomatic infections.The mechanisms by which biofilm formation occurs and are regulated are not completely understood in the Bordetella species, although several pathways and important components of the biofilm have been identified. One of the major observations that inspired this work was that a B. bronchiseptica strain from III which the cyaA gene, encoding adenylate cyclase toxin (ACT), has been deleted, formed more biofilm than wild type bacteria, suggesting the possibility of an inhibitory effect of ACT. ACT is a host-directed, protein, bacterial toxin, and the toxin's role as an inhibitor of biofilm is unprecedented. It was also discovered by Zaretzky et al that ACT binds Filamentous Hemagglutinin (FHA), a surface displayed adhesin required for biofilm formation. Until now, the consequences of this interaction were unknown. We have found that ACT binds to FHA via a direct interaction between the catalytic domain of ACT (AC domain) and the mature cterminal domain of FHA (MCD). This protein-protein interaction results in the inhibition and disruption of biofilm formation. The AC domain is also able to inhibit biofilm of other bacterial species that express an FHA-like protein.In fitting these findings into the overall body of knowledge regarding Bordetellae biofilm, we found major differences in the regulatory processes controlling B. bronchiseptica and B. pertussis biofilm. Flagella are essential for initial binding and mature biofilm formation by B. bronchiseptica. In contrast, B. pertussis forms biofilm despite being classically defined as a non-motile and nonflagellated bacterium. B. pertussis encodes all of the required ge...

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Identification of a Hemagglutinin from Gallibacterium anatis

Cited by 9 publications

References 22 publications

A putative siderophore receptor of Gallibacterium anatis 12656-12 under Fur control also binds hemoglobin

A putative siderophore receptor of Gallibacterium anatis 12656-12 under Fur control also binds hemoglobin

Characterization of Actinobacillus seminis biofilm formation

The "Mystery Phases": Bordetella Adenylate Cyclase Toxin and biofilm in the Bvg-Intermediate Phase & Bordetella pertussis Motility and Flagella in the Bvg-Minus Phase

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