ライフサイエンスコーパス: M. haemolytica

1 M. haemolytica is one of the causative agents of bovine

2 M. haemolytica is surrounded by a polysaccharide capsule

3 Currently used vaccines against M. haemolytica do not provide complete protection agains

4 -kDa protein band is recognized by both anti-M. haemolytica OmpA and anti-Lpp1 antibodies.

5 tro and that adherence was inhibited by anti-M. haemolytica antibody.

6 , and IV alleles were associated with bovine M. haemolytica, ovine M. haemolytica, and M. glucosida s

7 precise subunit of bovine LFA-1 utilized by M. haemolytica Lkt as the functional receptor.

8 as class III alleles were present in certain M. haemolytica and M. glucosida isolates.

9 tegral to PMN recruitment to the lung during M. haemolytica infection.

10 n to previously described virulence factors, M. haemolytica encodes adhesins, including the filamento

11 inding specificities of these antibodies for M. haemolytica isolates representing different OmpA subc

12 (2)-integrins is the functional receptor for M. haemolytica Lkt.

13 es to determine the role of sRNA, if any, in M. haemolytica pathogenesis.

14 ' ends of the operon are highly conserved in M. haemolytica, which suggests that multiple horizontal

15 ntrast, the lktD gene is highly conserved in M. haemolytica.

16 lso contributed to strain diversification in M. haemolytica.

17 classes, classes I to IV, were identified in M. haemolytica and M. glucosida.

18 usions, to study transcription initiation in M. haemolytica.

19 ible for the severity of the lung lesions in M. haemolytica-infected BHS.

20 anti-Lpp1 antibodies significantly inhibited M. haemolytica binding to BBEC monolayers.

21 ukotoxin expression may provide insight into M. haemolytica pathogenicity.

22 BHS and DS were stimulated with heat-killed M. haemolytica or LPS.

23 ainst the R2 region are effective in killing M. haemolytica.

24 not necessary for the cytotoxic activity of M. haemolytica Lkt but that it enhances the potency of t

25 hat OmpA and Lpp1 contribute to adherence of M. haemolytica to bovine respiratory epithelial cells.

26 Western blot analysis of M. haemolytica proteins that bind to BBEC showed a domin

27 interferon (IFN-gamma) on the interaction of M. haemolytica LKT with bovine peripheral blood neutroph

28 enhanced subsequent trapping and killing of M. haemolytica cells in bovine NETs.

29 among the different evolutionary lineages of M. haemolytica.

30 we demonstrate that the leukotoxin (LKT) of M. haemolytica causes NET formation by bovine neutrophil

31 lytic pro-LKT (produced by an lktC mutant of M. haemolytica) stimulated MET formation.

32 c pro-LKT produced by an DeltalktC mutant of M. haemolytica, we show that binding of unacylated pro-L

33 The leukotoxin operon of M. haemolytica has a complex mosaic structure and has be

34 es should reveal whether the presentation of M. haemolytica leukotoxin peptides to T(h) cells by Ovca

35 It is proposed that the OmpA protein of M. haemolytica acts as a ligand and is involved in bindi

36 The OmpA proteins of M. haemolytica and M. glucosida contain four hypervariab

37 he polysaccharide capsule, in a selection of M. haemolytica isolates of various serotypes and grown u

38 of the leukotoxin operon in ovine strains of M. haemolytica.

39 ompA genes are highly diverged from those of M. haemolytica and M. glucosida, and evidence is present

40 Lesional lung tissue of M. haemolytica-infected BHS contained significantly high

41 reduced NET formation in response to LKT or M. haemolytica cells.

42 mains of OmpA proteins from bovine and ovine M. haemolytica isolates are very different but are highl

43 e specificity of OmpA among bovine and ovine M. haemolytica isolates, recombinant proteins representi

44 with divergent lineages of bovine and ovine M. haemolytica strains, respectively, indicating a histo

45 associated with bovine M. haemolytica, ovine M. haemolytica, and M. glucosida strains, respectively,

46 In this study, we demonstrated that M. haemolytica adhered to bovine bronchial epithelial ce

47 vious studies by us and others indicate that M. haemolytica Lkt binds to CD18, the beta subunit of bo

48 Analysis of the genome indicates that M. haemolytica is naturally competent, as genes for natu

49 in the family Pasteurellaceae indicates that M. haemolytica, Actinobacillus pleuropneumoniae, and Hae

50 Recent evidence suggests that M. haemolytica LKT binding to bovine leukocytes is media

51 e to LKT trapped and killed a portion of the M. haemolytica cells.

52 s-in-toxin (RTX) toxin family related to the M. haemolytica leukotoxin.

53 vine monocyte-derived macrophages exposed to M. haemolytica or its LKT.

54 ng the biological response of bovine PMNs to M. haemolytica LKT.

55 ing lines of cattle genetically resistant to M. haemolytica-caused pneumonia, which inflicts an econo

56 Understanding NET formation in response to M. haemolytica and its LKT provides a new perspective on

57 ion revealed that NETs formed in response to M. haemolytica are capable of trapping and killing a por

58 d monocytes, also formed METs in response to M. haemolytica cells.

59 phages and PMNs of BHS and DS in response to M. haemolytica.

60 (BHS), since they are highly susceptible to M. haemolytica infection.

61 ed a function and 436 of which are unique to M. haemolytica.

62 graphy-tandem mass spectrometry, matched two M. haemolytica surface proteins: heat-modifiable outer m

63 Research with M. haemolytica outer membrane proteins (OMPs) has shown