ライフサイエンスコーパス: haemolytica

1 s somnus, Neisseria species, and Pasteurella haemolytica.

2 ) and CD18(-) cattle after inoculation of P. haemolytica.

3 antibody titers against RBCV and Pasteurella haemolytica.

4 t PlpE contribute to host defense against P. haemolytica.

5 elium after acute infection with Pasteurella haemolytica.

6 [32K and 35K, respectively]) of Pasteurella haemolytica.

7 eria meningitidis, and LpsA from Pasteurella haemolytica.

8 ges and PMNs of BHS and DS in response to M. haemolytica.

9 y the bovine respiratory pathogen Mannheimia haemolytica.

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

11 kotoxin secreted by Mannheimia (Pasteurella) haemolytica.

12 st the R2 region are effective in killing M. haemolytica.

13 contributed to strain diversification in M. haemolytica.

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

15 ng the different evolutionary lineages of M. haemolytica.

16 ons, to study transcription initiation in M. haemolytica.

17 ast, the lktD gene is highly conserved in M. haemolytica.

18 after respiratory infection with Pasteurella haemolytica.

19 investigated in 31 Mannheimia (Pasteurella) haemolytica, 6 Mannheimia glucosida, and 4 Pasteurella t

20 nd lktD genes in 23 Mannheimia (Pasteurella) haemolytica, 6 Mannheimia glucosida, and 4 Pasteurella t

21 Mannheimia haemolytica, a commensal organism of the upper respirato

22 A Pasteurella haemolytica A1 gene was identified from a recombinant li

23 Mannheimia (Pasteurella) haemolytica A1 produces several virulence factors that p

24 mal CD18 expression) were inoculated with P. haemolytica A1 via a fiberoptic bronchoscope and euthani

25 The draft genome sequence of Mannheimia haemolytica A1, the causative agent of bovine respirator

26 otective antigen for GBM, E. coli K1, and P. haemolytica A2, protein conjugates of it are easy to pre

27 (GBMs), Escherichia coli K1, and Pasteurella haemolytica A2.

28 the family Pasteurellaceae indicates that M. haemolytica, Actinobacillus pleuropneumoniae, and Haemop

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

30 In this study, we demonstrated that M. haemolytica adhered to bovine bronchial epithelial cells

31 ndicating that PlpE is surface exposed in P. haemolytica and assumes a similar surface-exposed confor

32 d be useful for future genetic studies in P. haemolytica and could potentially be applied to other me

33 of all known Hsd aa sequences placed the P. haemolytica and H. influenzae proteins into a new group

34 n vectors that replicate both in Pasteurella haemolytica and in Escherichia coli were constructed bas

35 he important respiratory pathogen Mannheimia haemolytica and its leukotoxin (LKT).

36 nderstanding NET formation in response to M. haemolytica and its LKT provides a new perspective on ho

37 The OmpA proteins of M. haemolytica and M. glucosida contain four hypervariable

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

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

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

41 (zinc saline solution) induced killing of P. haemolytica and other bacteria comparable to defensins a

42 We found that intact P. haemolytica and recombinant E. coli expressing PlpE are

43 our matched pairs of isolates of Pasteurella haemolytica and three matched pairs of isolates of Paste

44 uantitate leukotoxin promoter activity in P. haemolytica and to demonstrate that transcription was ma

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

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

47 inning, while their antibody responses to P. haemolytica antigens were delayed.

48 revealed that NETs formed in response to M. haemolytica are capable of trapping and killing a portio

49 i-Lpp1 antibodies significantly inhibited M. haemolytica binding to BBEC monolayers.

50 The leukotoxin (LktA) produced by Mannheimia haemolytica binds to bovine lymphocyte function-associat

51 kotoxin secreted by Mannheimia (Pasteurella) haemolytica binds to the intact signal peptide and cause

52 was surface exposed, was conserved among P. haemolytica biotype A serotypes, and had porin activity

53 PomB, respectively), were extracted from P. haemolytica by solubilization in N-octyl polyoxyl ethyle

54 d streptomycin (SmR) resistant plasmid of P. haemolytica called pYFC1.

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

56 demonstrate that the leukotoxin (LKT) of M. haemolytica causes NET formation by bovine neutrophils i

57 Mannheimia haemolytica causes pneumonia in domestic and wild rumina

58 hanced subsequent trapping and killing of M. haemolytica cells in bovine NETs.

59 e different bovine immune sera with whole P. haemolytica cells resulted in a reduction of bovine immu

60 o LKT trapped and killed a portion of the M. haemolytica cells.

61 duced NET formation in response to LKT or M. haemolytica cells.

62 onocytes, also formed METs in response to M. haemolytica cells.

63 istically with resistance to experimental P. haemolytica challenge in cattle.

64 A Pasteurella haemolytica cosmid clone that activates leukotoxin trans

65 Cattle vaccinated with live P. haemolytica developed a significant increase in serum an

66 Currently used vaccines against M. haemolytica do not provide complete protection against t

67 o previously described virulence factors, M. haemolytica encodes adhesins, including the filamentous

68 s recognize a protein in all serotypes of P. haemolytica except serotype 11.

69 consequence of the unusual codon usage in P. haemolytica genes.

70 The leukotoxin operon of M. haemolytica has a complex mosaic structure and has been

71 n of chromosomal gene fusions in Pasteurella haemolytica has been devised and used to create an lktC:

72 ) system of the bovine pathogen, Pasteurella haemolytica, have been identified immediately downstream

73 The P. haemolytica hsdMSR genes were mapped using transposon Tn

74 c lesions and mortality caused by Mannheimia haemolytica in bighorn sheep (BHS; Ovis canadensis) are

75 ole for the lipopolysaccharide (LPS) from P. haemolytica in the induction of proinflammatory cytokine

76 P. haemolytica incubated with H-DDDDDD-OH in zinc saline so

77 Lesional lung tissue of M. haemolytica-infected BHS contained significantly higher

78 e for the severity of the lung lesions in M. haemolytica-infected BHS.

79 ression of PIC was induced at 2 h p.i. in P. haemolytica-infected cattle and continued to 4 h p.i.

80 ral to PMN recruitment to the lung during M. haemolytica infection.

81 HS), since they are highly susceptible to M. haemolytica infection.

82 on of some PIC genes, as a consequence of P. haemolytica infection.

83 and TNF-alpha genes were not increased in P. haemolytica-inoculated CD18(-) cattle lungs compared to

84 The induction of gene expression with P. haemolytica inoculation was more prominent in CD18(-) ca

85 Mannheimia haemolytica is a key pathogen in the bovine respiratory

86 Mannheimia haemolytica is an important member of the bovine respira

87 Pasteurella haemolytica is an important respiratory pathogen of catt

88 The leukotoxin of Mannheimia haemolytica is an important virulence factor that contri

89 n (Lkt) secreted by Mannheimia (Pasteurella) haemolytica is an RTX toxin which is specific for rumina

90 The leukotoxin of Pasteurella (Mannheimia) haemolytica is believed to play a significant role in pa

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

92 M. haemolytica is one of the causative agents of bovine res

93 M. haemolytica is surrounded by a polysaccharide capsule, a

94 Mannheimia haemolytica is the etiological agent of pneumonic pasteu

95 nant-specific leukotoxin (Lkt) of Mannheimia haemolytica is the key virulence factor contributing to

96 Pasteurella haemolytica is the principal bacterial pathogen in the b

97 Mannheimia haemolytica is the principal bacterial pathogen of the b

98 ns of OmpA proteins from bovine and ovine M. haemolytica isolates are very different but are highly c

99 polysaccharide capsule, in a selection of M. haemolytica isolates of various serotypes and grown unde

100 ing specificities of these antibodies for M. haemolytica isolates representing different OmpA subclas

101 pecificity of OmpA among bovine and ovine M. haemolytica isolates, recombinant proteins representing

102 different ribotypes were observed for the P. haemolytica isolates, while only one ribotype was observ

103 cent reports have shown that the Pasteurella haemolytica leukotoxin (LKT) and other RTX toxins bind b

104 Pasteurella (Mannheimia) haemolytica leukotoxin (Lkt) causes cell type- and speci

105 S) preparations of the RTX toxin Pasteurella haemolytica leukotoxin (LKT) contained LKT and LPS as th

106 The effects of Pasteurella haemolytica leukotoxin (LKT) on the activity of phosphol

107 xposure of bovine neutrophils to Pasteurella haemolytica leukotoxin (LKT) stimulates the production o

108 inant leukocytes to Mannheimia (Pasteurella) haemolytica leukotoxin (Lkt).

109 wo other RTX toxin proteins, the Pasteurella haemolytica leukotoxin (LktA) and the enterohemorrhagic

110 To map the site involved in Mannheimia haemolytica leukotoxin (LktA) binding and biological act

111 Incubation of bovine leukocytes with P. haemolytica leukotoxin caused marked cytoplasmic membran

112 at encodes a transcriptional activator of P. haemolytica leukotoxin expression.

113 there may be a specific binding site for P. haemolytica leukotoxin on bovine but not on porcine or h

114 should reveal whether the presentation of M. haemolytica leukotoxin peptides to T(h) cells by Ovca-DR

115 The related RTX toxin, the Pasteurella haemolytica leukotoxin structural protein (LktA), can be

116 lower titer of antibodies against Mannheimia haemolytica leukotoxin, in comparison to domestic sheep

117 n-toxin (RTX) toxin family related to the M. haemolytica leukotoxin.

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

119 Recent evidence suggests that M. haemolytica LKT binding to bovine leukocytes is mediated

120 Therefore, P. haemolytica LKT binds rapidly to susceptible and to repu

121 Recent studies indicate that P. haemolytica Lkt binds to bovine CD18, the common subunit

122 us studies by us and others indicate that M. haemolytica Lkt binds to CD18, the beta subunit of bovin

123 t necessary for the cytotoxic activity of M. haemolytica Lkt but that it enhances the potency of the

124 erferon (IFN-gamma) on the interaction of M. haemolytica LKT with bovine peripheral blood neutrophils

125 -integrins is the functional receptor for M. haemolytica Lkt.

126 the biological response of bovine PMNs to M. haemolytica LKT.

127 In this study, the P. haemolytica lktC mutant was shown to be less virulent th

128 Our findings support a role for P. haemolytica LPS and TNF-alpha in the induction of IL-8 f

129 d the kinetics of IL-8 mRNA expression in P. haemolytica LPS-stimulated bovine alveolar macrophages a

130 ymal damage caused by factors released by P. haemolytica, neutrophils contribute to the pathologic ch

131 a protein band is recognized by both anti-M. haemolytica OmpA and anti-Lpp1 antibodies.

132 Until now, specific P. haemolytica OMPs which elicit antibodies that function i

133 less cat cassette and then delivered into P. haemolytica on a shuttle vector.

134 e monocyte-derived macrophages exposed to M. haemolytica or its LKT.

135 S and DS were stimulated with heat-killed M. haemolytica or LPS.

136 tis, bovine viral diarrhea virus, Mannheimia haemolytica or Mycoplasma bovis.

137 The presence of antibodies against P. haemolytica outer membrane proteins (OMPs) correlates st

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

139 represent an important mechanism by which P. haemolytica overwhelms host defenses, contributing to th

140 nd IV alleles were associated with bovine M. haemolytica, ovine M. haemolytica, and M. glucosida stra

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

142 toxin expression may provide insight into M. haemolytica pathogenicity.

143 existing structural annotation of Mannheimia haemolytica PHL213 based on experimental evidence.

144 isit the structural annotation of Mannheimia haemolytica PHL213, a bovine respiratory disease pathoge

145 osome by Cre recombinase expressed from a P. haemolytica plasmid.

146 rophil infiltration into the lungs during P. haemolytica pneumonia are poorly characterized.

147 d from neonatal calves with acute Mannheimia haemolytica pneumonia showed that rapid up-regulation of

148 ramphenicol resistance gene (cat, CmR) in P. haemolytica (pNF2200).

149 Western blot analysis of M. haemolytica proteins that bind to BBEC showed a dominant

150 Expression of the P. haemolytica R-M genes in E. coli was inefficient and is

151 nfection of the bovine lung with Pasteurella haemolytica results in an acute respiratory disorder kno

152 Of the six P. haemolytica ribotypes, two ribotypes predominated.

153 Plasmid pNF2176 carries the P. haemolytica ROB-1 beta-lactamase gene (blaP, ApR) and pN

154 Mannheimia haemolytica serotype 1 (S1) is the most common bacterial

155 toxin and endotoxin derived from Pasteurella haemolytica serotype 1 are the primary virulence factors

156 Pasteurella haemolytica serotype 1 is the bacterial agent responsibl

157 Pasteurella haemolytica serotype 1 is the bacterium most commonly as

158 Pasteurella haemolytica serotype A1 (bovine strain OK) was incubated

159 describes the genome sequences of Mannheimia haemolytica serotype A2 isolated from pneumonic lungs of

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

161 The P. haemolytica strain used was a mutant serotype A1 from wh

162 th divergent lineages of bovine and ovine M. haemolytica strains, respectively, indicating a history

163 phy-tandem mass spectrometry, matched two M. haemolytica surface proteins: heat-modifiable outer memb

164 lture supernatant from a mutant strain of P. haemolytica that does not produce any detectable leukoto

165 culture filtrates from a mutant strain of P. haemolytica that does not produce biologically active le

166 Pasteurella haemolytica, the causative agent of shipping fever pneum

167 hi and bronchioles of lungs infected with P. haemolytica, three Holstein calves homozygous for bovine

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

169 Cattle were infected with P. haemolytica via fiberoptic deposition of organisms into

170 e lungs of CD18(+) cattle inoculated with P. haemolytica was greater than that in lungs of the CD18(-

171 ural gene (lktA) of Mannheimia (Pasteurella) haemolytica was investigated by nucleotide sequence comp

172 the bovine respiratory pathogen Pasteurella haemolytica, was cloned, and its nucleotide sequence was

173 ro-LKT produced by an DeltalktC mutant of M. haemolytica, we show that binding of unacylated pro-LKT

174 ved a significant reduction in killing of P. haemolytica when bovine immune serum that was depleted o

175 y surfactant is bactericidal for Pasteurella haemolytica when surfactant and bacteria mixtures are in

176 nds of the operon are highly conserved in M. haemolytica, which suggests that multiple horizontal exc