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 t the explosive proliferation of serotype A1 M. haemolytica that occurs within the bovine respiratory

4 e demonstrated that serotype A1, but not A2, M. haemolytica invades differentiated BBECs by transcyto

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

6 %) than in Control calves (10.4%) on d2, and M. haemolytica prevalence on d7 as compared to control c

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

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

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

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

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

12 ng in the bloodstream of dairy calves during M. haemolytica infection are reflected in the NIR spectr

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

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

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

16 (75%), while fewer calves were positive for M. haemolytica (13%).

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

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

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

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

21 lso contributed to strain diversification in M. haemolytica.

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

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

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

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

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

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

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

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

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

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

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

33 ry little is known about the interactions of M. haemolytica with airway epithelial cells of the respi

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

35 among the different evolutionary lineages of M. haemolytica.

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

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

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

39 ts indicate that the host-specific nature of M. haemolytica infection may result at least partially f

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

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

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

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

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

45 inoculated with serotype A1 or A2 strains of M. haemolytica and the course of infection followed over

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

47 ective, reproducible models for the study of M. haemolytica pathogenesis has hampered efforts to bett

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

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

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

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

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

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

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

55 ion of various pathogenic and non-pathogenic M. haemolytica isolates of bovine and ovine origin.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

73 blood plasma from dairy calves infected with M. haemolytica and validates the spectral biochemistry u

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