Open Access
Vet. Res.
Volume 41, Number 3, May–June 2010
Number of page(s) 14
Published online 04 December 2009
How to cite this article Vet. Res. (2010) 41:25
  • Altschul S.F., Madden T.L., Schaffer A.A., Zhang J.H., Zhang Z., Miller W., Lipman D.J., Gapped BLAST and PSI-BLAST: a new generation of protein database search programs, Nucleic Acids Res. (1997) 25:3389–3402. [CrossRef] [PubMed] [Google Scholar]
  • Barany F., Two-codon insertion mutagenesis of plasmid genes by using single-stranded hexameric oligonucleotides, Proc. Natl. Acad. Sci. USA (1985) 82:4202–4206. [CrossRef] [Google Scholar]
  • Beug H., Vonkirchbach A., Doderlein G., Conscience J.F., Graf T., Chicken hematopoietic-cells transformed by 7 strains of defective avian leukemia viruses display 3 distinct phenotypes of differentiation, Cell (1979) 18:375–390. [CrossRef] [PubMed] [Google Scholar]
  • Bisgaard M., Dam A., Salpingitis in poultry. II. Prevalence, bacteriology, and possible pathogenesis in egg-laying chickens, Nord. Vet. Med. (1981) 33:81–89. [PubMed] [Google Scholar]
  • Bojesen A.M., Torpdahl M., Christensen H., Olsen J.E., Bisgaard M., Genetic diversity of Gallibacterium anatis isolates from different chicken flocks, J. Clin. Microbiol. (2003) 41:2737–2740. [CrossRef] [PubMed] [Google Scholar]
  • Bojesen A.M., Nielsen S.S., Bisgaard M., Prevalence and transmission of haemolytic Gallibacterium species in chicken production systems with different biosecurity levels, Avian Pathol. (2003) 32:503–510. [CrossRef] [PubMed] [Google Scholar]
  • Bojesen A.M., Christensen J.P., Bisgaard M., Gallibacterium infections and other avian Pasteurellaceae, in: Pattison M., Mcmullin P.F., Bradbury J.M., Alexander D.J. (Eds.), Poultry diseases, Saunders Elsevier, Edinburg, 2008, pp. 160–163. [CrossRef] [Google Scholar]
  • Bulach D.M., Zuerner R.L., Wilson P., Seemann T., McGrath A., Cullen P.A., et al., Genome reduction in Leptospira borgpetersenii reflects limited transmission potential, Proc. Natl. Acad. Sci. USA (2006) 103:14560–14565. [CrossRef] [Google Scholar]
  • Christensen H., Bisgaard M., Bojesen A.M., Mutters R., Olsen J.E., Genetic relationships among avian isolates classified as Pasteurella haemolytica, “Actinobacillus salpingitidis” or Pasteurella anatis with proposal of Gallibacterium anatis gen. nov., comb. nov. and description of additional genomospecles within Gallibacterium gen. nov, Int. J. Syst. Evol. Microbiol. (2003) 53:275–287. [CrossRef] [PubMed] [Google Scholar]
  • Frees D., Chastanet A., Qazi S., Sorensen K., Hill P., Msadek T., Ingmer H., Clp ATPases are required for stress tolerance, intracellular replication and biofilm formation in Staphylococcus aureus, Mol. Microbiol. (2004) 54:1445–1462. [CrossRef] [PubMed] [Google Scholar]
  • Frey J., Kuhnert P., RTX toxins in Pasteurellaceae, Int. J. Med. Microbiol. (2002) 292:149–158. [CrossRef] [PubMed] [Google Scholar]
  • Garcia-Gomez E., Vaca S., Perez-Mendez A., Ibarra-Caballero J., Perez-Marquez V., Tenorio V.R., Negrete-Abascal E., Gallibacterium anatis-secreted metalloproteases degrade chicken IgG, Avian Pathol. (2005) 34:426–429. [CrossRef] [PubMed] [Google Scholar]
  • Gerlach H., Die Bedeutung von Pasteurella haemolytica in Hühnerbeständen, Prakt. Tierarzt (1977) 5:324–328. [Google Scholar]
  • Greenham L.W., Hill T.J., Observations on an avian strain of Pasteurella haemolytica, Vet. Rec. (1962) 74:861–863. [Google Scholar]
  • Harry E.G., A haemolytic coccobacillus recovered from poultry, Vet. Rec. (1962) 74:640. [Google Scholar]
  • Heger A., Holm L., Rapid automatic detection and alignment of repeats in protein sequences, Proteins (2000) 41:224–237. [CrossRef] [PubMed] [Google Scholar]
  • Hinz K.H., Bakteriologische Befunde bei Erkrankungen der Atmungsorgane von Junghennen, 9th Congress of the World Veterinary Poultry Association, Beograd, 1969, pp. 713–718. [Google Scholar]
  • Horton R.M., Cai Z.L., Ho S.N., Pease L.R., Gene-splicing by overlap extension: tailor-made genes using the polymerase chain-reaction, Biotechniques (1990) 8:528–535. [PubMed] [Google Scholar]
  • Jansen R., Briaire J., Smith H.E., Dom P., Haesebrouck F., Kamp E.M., , Knockout mutants of Actinobacillus pleuropneumoniae serotype 1 that are devoid of Rtx toxins do not activate or kill porcine neutrophils, Infect. Immun. (1995) 63:27–37. [PubMed] [Google Scholar]
  • Jarma E., Regassa L.B., Growth phase mediated regulation of the Actinobacillus pleuropneumoniae ApxI and ApxII toxins, Microb. Pathog. (2004) 36:197–203. [CrossRef] [PubMed] [Google Scholar]
  • Jordan F.T., Williams N.J., Wattret A., Jones T., Observations on salpingitis, peritonitis and salpingoperitonitis in a layer breeder flock, Vet. Rec. (2005) 157:573–577. [PubMed] [Google Scholar]
  • Kamp E.M., Popma J.K., Anakotta J., Smits M.A., Identification of hemolytic and cytotoxic proteins of Actinobacillus pleuropneumoniae by use of monoclonal antibodies, Infect. Immun. (1991) 59:3079–3085. [PubMed] [Google Scholar]
  • Kingsford C.L., Ayanbule K., Salzberg S.L., Rapid, accurate, computational discovery of Rho-independent transcription terminators illuminates their relationship to DNA uptake, Genome Biol. (2007) 8:R22. [CrossRef] [PubMed] [Google Scholar]
  • Kjos-Hanssen B., Egglederperitonitt forårsaket av patogen “kloakkbakterie” hos høns, Nord. Vet. Med. (1950) 2:523–531. [Google Scholar]
  • Kohlert R., Untersuchungen zur ätiologie der Eileiterentzündung beim Huhn, Monatsh. Veterinärmed. (1967) 23:392–395. [Google Scholar]
  • Mackman N., Nicaud J.M., Gray L., Holland I.B., Genetical and functional organisation of the Escherichia coli haemolysin determinant 2001, Mol. Gen. Genet. (1985) 201:282–288. [CrossRef] [PubMed] [Google Scholar]
  • Margulies M., Egholm M., Altman W.E., Attiya S., Bader J.S., Bemben L.A., et al., Genome sequencing in microfabricated high-density picolitre reactors, Nature (2005) 437:376–380. [PubMed] [Google Scholar]
  • Mirle C., Schöngarth M., Meinhart H., Olm U., Untersuchungen zu Auftreten und Bedeutung von Pasteurella haemolytica-Infektionen bei Hennen unter besonderer Berücksichtigung von Erkrankungen des Legesapparates, Monatsh. Veterinärmed. (1991) 46:545–549. [Google Scholar]
  • Neubauer C., De Souza-Pilz M., Bojesen A.M., Bisgaard M., Hess M., Tissue distribution of haemolytic Gallibacterium anatis isolates in laying birds with reproductive disorders, Avian Pathol. (2008) 38:1–7. [CrossRef] [Google Scholar]
  • Pearson W.R., Lipman D.J., Improved tools for biological sequence comparison, Proc. Natl. Acad. Sci. USA (1988) 85:2444–2448. [CrossRef] [Google Scholar]
  • Poje G., Redfield R.J., Transformation of Haemophilus influenzae, Methods Mol. Med. (2003) 71:57–70. [PubMed] [Google Scholar]
  • Reimer D., Frey J., Jansen R., Veit H.P., Inzana T.J., Molecular investigation of the role of ApxI and ApxII in the virulence of Actinobacillus pleuropneumoniae serotype 5, Microb. Pathog. (1995) 18:197–209. [CrossRef] [PubMed] [Google Scholar]
  • Rowe G.E., Welch R.A., Assays of hemolytic toxins, Methods Enzymol. (1994) 235:657–667. [CrossRef] [PubMed] [Google Scholar]
  • Sakamoto H., Bellalou J., Sebo P., Ladant D., Bordetella pertussis adenylate cyclase toxin. Structural and functional independence of the catalytic and hemolytic activities, J. Biol. Chem. (1992) 267:13598–13602. [PubMed] [Google Scholar]
  • Schaller A., Kuhn R., Kuhnert P., Nicolet J., Anderson T.J., MacInnes J.I., , Characterization of apxIVA, a new RTX determinant of Actinobacillus pleuropneumoniae, Microbiology (1999) 145:2105–2116. [CrossRef] [PubMed] [Google Scholar]
  • Soding J., Biegert A., Lupas A.N., The HHpred interactive server for protein homology detection and structure prediction, Nucleic Acids Res. (2005) 33:W244–W248. [CrossRef] [PubMed] [Google Scholar]
  • Stanley P., Packman L.C., Koronakis V., Hughes C., Fatty acylation of 2 internal lysine residues required for the toxic activity of Escherichia coli hemolysin, Science (1994) 266:1992–1996. [CrossRef] [PubMed] [Google Scholar]
  • Strathdee C.A., Lo R.Y., Regulation of expression of the Pasteurella haemolytica leukotoxin determinant, J. Bacteriol. (1989) 171:5955–5962. [PubMed] [Google Scholar]
  • Tascon R.I., Vazquez-Boland J.A., Gutierrez-Martin C.B., Rodriguez-Barbosa I., Rodriguez-Ferri E.F., The RTX haemolysins ApxI and ApxII are major virulence factors of the swine pathogen Actinobacillus pleuropneumoniae: evidence from mutational analysis, Mol. Microbiol. (1994) 14:207–216. [CrossRef] [PubMed] [Google Scholar]
  • Tatum F.M., Briggs R.E., Sreevatsan S.S., Zehr E.S., Ling Hsuan S., Whiteley L.O., , Construction of an isogenic leukotoxin deletion mutant of Pasteurella haemolytica serotype 1: characterization and virulence, Microb. Pathog. (1998) 24:37–46. [CrossRef] [PubMed] [Google Scholar]
  • Vojtova J., Kamanova J., Sebo P., Bordetella adenylate cyclase toxin: a swift saboteur of host defense, Curr. Opin. Microbiol. (2006) 9:69–75. [CrossRef] [PubMed] [Google Scholar]
  • Wang R.F., Kushner S.R., Construction of versatile low-copy-number vectors for cloning, sequencing and gene expression in Escherichia coli, Gene (1991) 100:195–199. [CrossRef] [PubMed] [Google Scholar]