Role of intracellular calcium in Pasteurella haemolytica leukotoxin-induced bovine neutrophil leukotriene B4 production and plasma membrane damage

Cudd, Laura

doi:10.1016/s0378-1097(99)00025-7

Cited by 8 publications

(19 citation statements)

References 9 publications

(20 reference statements)

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“…M. haemolytica infection induces release of IL-1, TNF-α and IL-8 by lung tissue [21,22] and initiates a profound procoagulant state resulting in extensive fibrin polymerization [23]. Other inflammtory mediators released by bovine lung in response to M. haemolytica products (LPS and LKT) include leukotriene B4, histamine and prostaglandin E2 [24,25]. A wide-spreading cascade of other cytokines and inflammatory mediators are likely released during acute M. haemolytica pneumonia and would likely include platelet-activating factor; however, only a small subset of these factors has been characterized in experimental conditions.…”

Section: Inflammatory Process Initiated By M Haemolyticamentioning

confidence: 99%

Response of the ruminant respiratory tract to

Ackermann

Brogden

2000

Microbes and Infection

138

103

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Pneumonia is a leading cause of loss to the sheep and cattle industry throughout the world. Mannheimia (Pasteurella) haemolytica is one of the most important respiratory pathogens of domestic ruminants and causes serious outbreaks of acute pneumonia in neonatal, weaned and growing lambs, calves, and goats.M. haemolytica is also an important cause of pneumonia in adult animals. Transportation, viral infections with agents such as infectious bovine rhinotracheitis virus, parainfluenza-3 virus or bovine respiratory syncytial virus, overcrowding, housing of neonates and weaned animals together and other stressful conditions predispose animals to M. haemolytica infection. This review assimilates some of the findings key to cellular and molecular responses of the lung from a pathologist′s perspective. It includes some of what is known and underscores areas that are not fully understood. Keywordsantimicrobial peptides, inflammation, innate immunity, pneumonia, pulmonary pasteurellosis Disciplines Veterinary Pathology and Pathobiology CommentsThis article is from Microbes and Infection 2, no. 9 ( July 2000): 1079-1088, doi:10.1016/ S1286-4579(00)01262-4. RightsWorks produced by employees of the U.S. Government as part of their official duties are not copyrighted within the U.S. The content of this document is not copyrighted. ABSTRACT -Pneumonia is a leading cause of loss to the sheep and cattle industry throughout the world. Mannheimia (Pasteurella) haemolytica is one of the most important respiratory pathogens of domestic ruminants and causes serious outbreaks of acute pneumonia in neonatal, weaned and growing lambs, calves, and goats. M. haemolytica is also an important cause of pneumonia in adult animals. Transportation, viral infections with agents such as infectious bovine rhinotracheitis virus, parainfluenza-3 virus or bovine respiratory syncytial virus, overcrowding, housing of neonates and weaned animals together and other stressful conditions predispose animals to M. haemolytica infection

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Section: Inflammatory Process Initiated By M Haemolyticamentioning

confidence: 99%

Response of the ruminant respiratory tract to

Ackermann

Brogden

2000

Microbes and Infection

138

103

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“…High doses of Lkt cause the lysis of ruminant leukocytes by membrane pore formation when paralleled by a rise in intracellular calcium levels (11,12,45,52). Lower doses of Lkt are chemotactic and stimulate active degranulation of bovine neutrophils in vitro (32,36).…”

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confidence: 99%

Potential Involvement of Gelatinases and Their Inhibitors inMannheimia haemolyticaPneumonia in Cattle

Starr¹,

Dan²,

Minhas³

et al. 2004

Infect Immun

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Mannheimia haemolytica infection of the lower respiratory tract of cattle results in a bronchofibrinous pneumonia characterized by massive cellular influx and lung tissue remodeling and scarring. Since altered levels of gelatinases and their inhibitors have been detected in a variety of inflammatory conditions and are associated with tissue remodeling, we examined the presence of gelatinases in lesional and nonlesional lung tissue obtained from calves experimentally infected with M. haemolytica. Lesional tissue had elevated levels of progelatinase A and B and active gelatinase A and B when compared with nonlesional tissue obtained from the same lung lobe. In vitro, M. haemolytica products stimulated production of gelatinase B, but not its activation, by bovine monocytes. Alveolar macrophages showed constitutive production of gelatinase B but no change in response to M. haemolytica products. Bovine neutrophils exposed to M. haemolytica products also released gelatinase B, and there was a significant increase in the activated form of this enzyme. These effects were virtually identical when recombinant O-sialoglycoprotease was used to stimulate these cells. M. haemolytica products also enhanced the expression by bovine monocytes and alveolar macrophages of the tissue inhibitor of metalloproteinase 1. Our results provide evidence that matrix metalloproteinases are activated in lung lesions from cattle with shipping fever and that M. haemolytica virulence products induce production, release, and especially activation of gelatinase B by bovine inflammatory cells in vitro.Bronchofibrinous pneumonia (shipping fever) is a respiratory disease in cattle that is characterized by cellular influx and interalveolar and interlobular fibrosis in the lungs of affected animals (3,7,18,20,64,65). Lung lesions consistently show areas of coagulation necrosis, extensive fibrin deposits, and intense cellular infiltration into the alveoli (5, 63, 65). Economic losses to the beef industry due to shipping fever are estimated at over one billion dollars per year in North America alone (64). Causes of this pneumonic condition are multifactorial, including a combination of stress or viral infection, with a final acute illness due most often to the bacteria Mannheimia (Pasteurella) haemolytica serotype A1 (16,39,64). M. haemolytica serotype A1 is a normal resident of the upper respiratory flora of most cattle, but when aspirated into the lower respiratory tract of immunocompromised animals, it is able to colonize the lungs and induce an inflammatory reaction (65).M. haemolytica was originally classified in the genus Pasteurella (50), but more recent genetic characterization has resulted in reclassification of 11 serotypes of biotype A in the new genus Mannheimia (4, 9). M. haemolytica is a trehalosenegative coccobacillus in which heat-stable lipopolysaccharide (LPS) constitutes 12 to 25% of the dried cell wall (66). During logarithmic growth, the bacteria produce and release a heatlabile exotoxin, termed leukotoxin (Lkt), and a heat-labile en...

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“…Earlier studies have demonstrated that the interaction of LktA with bovine leukocytes induces intracellular calcium ([Ca 2ϩ ] i ) elevation (9,17,21,22,36). Elevation of [Ca 2ϩ ] i appears to be critical for LktA-induced NF-B activation (21), proinflammatory cytokine gene expression (21), and arachidonic acid release and cytolysis (24).…”

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confidence: 99%

Mannheimia haemolyticaLeukotoxin Activates a Nonreceptor Tyrosine Kinase Signaling Cascade in Bovine Leukocytes, Which Induces Biological Effects

et al. 2001

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The leukotoxin (LktA) produced by Mannheimia haemolytica binds to bovine lymphocyte function-associated antigen 1 (LFA-1) and induces biological effects in bovine leukocytes in a cellular and species-specific fashion. We have previously shown that LktA also binds to porcine LFA-1 without eliciting any effects. These findings suggest that the specificity of LktA effects must entail both binding to LFA-1 and activation of signaling pathways which are present in bovine leukocytes. However, the signaling pathways leading to biological effects upon LktA binding to LFA-1 have not been characterized. In this context, several reports have indicated that ligand binding to LFA-1 results in activation of a nonreceptor tyrosine kinase (NRTK) signaling cascade. We designed experiments with the following objectives: (i) to determine whether LktA binding to LFA-1 leads to activation of NRTKs, (ii) to examine whether LktA-induced NRTK activation is target cell specific, and (iii) to determine whether LktA-induced NRTK activation is required for biological effects. We used a biologically inactive mutant leukotoxin ( Bovine pneumonic pasteurellosis (BPP) caused by Mannheimia (Pasteurella) haemolytica serotype 1 remains a major economic problem for the beef and dairy cattle industries in North America and Western Europe (2, 10, 14, 47). The leukotoxin (LktA) produced by this bacterium is the primary virulence factor that contributes to the pathogenesis of the fibrinonecrotizing pleuropneumonia and death characteristic of this disease (7,8,43,44). A large body of evidence indicates that much of the lung injury in this disease is caused by inflammatory mediators released from alveolar leukocytes by LktA-induced activation and cytolysis (11,34,41,48).LktA is a member of a family of gram-negative RTX (repeats in toxin) cytolysins (12,20). Unlike most other RTX cytolysins, leukotoxins produced by Actinobacillus actinomycetemcomitans (LtxA) and M. haemolytica (LktA) demonstrate cell-type-specific and species-specific biological effects. The LtxA of A. actinomycetemcomitans, which causes dental caries in humans, interacts only with cells of the lymphocytic and monomyelocytic lineages of humans and some nonhuman primates and provokes biological effects (29); the LktA of M. haemolytica interacts only with ruminant leukocytes and platelets and induces biological effects (6,25,37). A study by Lally et al. (30) reported that human lymphocyte function-associated antigen 1 (LFA-1), a member of the ␤2 integrins, is a target cell receptor for LtxA of A. actinomycetemcomitans. Three studies have identified bovine CD18, the ␤ subunit of all three bovine ␤2 integrins (LFA-1, Mac-1, and p150,95), as a receptor for M. haemolytica LktA (3,33,42). However, in these studies no specific member of the ␤2 integrin family was identified as an LktA receptor. We have extended these observations and have shown that bovine LFA-1, but not other members of the ␤2 integrin family, is a receptor for M. haemolytica LktA (23).LFA-1 is a heterodimeric glycoprotein co...

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Role of intracellular calcium in Pasteurella haemolytica leukotoxin-induced bovine neutrophil leukotriene B4 production and plasma membrane damage

Cited by 8 publications

References 9 publications

Response of the ruminant respiratory tract to

Response of the ruminant respiratory tract to

Potential Involvement of Gelatinases and Their Inhibitors inMannheimia haemolyticaPneumonia in Cattle

Mannheimia haemolyticaLeukotoxin Activates a Nonreceptor Tyrosine Kinase Signaling Cascade in Bovine Leukocytes, Which Induces Biological Effects

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