An analysis of the codon usage of Pasteurella haemolytica A1

Lo, R

doi:10.1016/0378-1097(92)90199-x

Cited by 3 publications

(3 citation statements)

References 9 publications

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“…Genes expressed at lower levels are not as likely to encounter dramatic selection pressures on translational efficiency and consequently show less bias in their patterns of codon usage. In addition, chromosomal position [43], G + C content [14,32,501, and safeguards against inappropriate expression of specialized genes [39] may also contribute to differential codon usage within a species. Therefore, a detailed study of codon usage within a protein coding sequence can often provide useful information about that gene.…”

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confidence: 99%

Analysis of Genomic G + C Content, Codon Usage, Initiator Codon Context and Translation Termination Sites In Tetrahymena Thermophila

Wuitschick

Karrer

1999

J Eukaryotic Microbiology

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In recent years, the amount of molecular sequencing data from Tetrahymena thermophila has dramatically increased. We analyzed G + C content, codon usage, initiator codon context and stop codon sites in the extremely A + T rich genome of this ciliate. Average G + C content was 38% for protein coding regions, 21% for 5' non-coding sequences, 19% for 3' non-coding sequences, 15% for introns, 19% for micronuclear limited sequences and 17% for macronuclear retained sequences flanking micronuclear specific regions. The 75 available T. thermophila protein coding sequences favored codons ending in T and, where possible, avoided those with G in the third position. Highly expressed genes were relatively G + C-rich and exhibited an extremely biased pattern of codon usage while developmentally regulated genes were more A + T-rich and showed less codon usage bias. Regions immediately preceding Tetrahymena translation initiator codons were generally A-rich. For the 60 stop codons examined, the frequency of G in the end + 1 site was much higher than expected whereas C never occupied this position.

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confidence: 99%

Analysis of Genomic G + C Content, Codon Usage, Initiator Codon Context and Translation Termination Sites In Tetrahymena Thermophila

Wuitschick

Karrer

1999

J Eukaryotic Microbiology

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“…Seven of the eight codons for the first glutamine of each repeat are CAG, whereas for the second glutamine, six of six codons are CAA. In P. haemolytica, CAA is the preferred codon for glutamine (26) and is reflective of the high moles percent AϩT content (ϳ60%) of P. haemolytica chromosomal DNA. For the first alanine in the repeat, six of six codons are GCA, whereas for the second alanine, five of seven codons are GCT.…”

Section: Discussionmentioning

confidence: 99%

Genetic and Immunologic Analyses of PlpE, a Lipoprotein Important in Complement-Mediated Killing ofPasteurella haemolyticaSerotype 1

1998

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Pasteurella haemolytica serotype 1 is the bacterium most commonly associated with bovine shipping fever. The presence of antibodies against P. haemolytica outer membrane proteins (OMPs) correlates statistically with resistance to experimental P. haemolytica challenge in cattle. Until now, specific P. haemolytica OMPs which elicit antibodies that function in host defense mechanisms have not been identified. In this study, we have cloned and sequenced the gene encoding one such protein, PlpE. Analysis of the deduced amino acid sequence revealed that PlpE is a lipoprotein and that it is similar to an Actinobacillus pleuropneumoniae lipoprotein, OmlA. Affinity-purified, anti-PlpE antibodies recognize a protein in all serotypes of P. haemolytica except serotype 11. We found that intact P. haemolytica and recombinant E. coli expressing PlpE are capable of absorbing anti-PlpE antibodies from bovine immune serum, indicating that PlpE is surface exposed in P. haemolytica and assumes a similar surface-exposed conformation in E. coli. In complement-mediated killing assays, we observed a significant reduction in killing of P. haemolytica when bovine immune serum that was depleted of anti-PlpE antibodies was used as the source of antibody. Our data suggest that PlpE is surface exposed and immunogenic in cattle and that antibodies against PlpE contribute to host defense against P. haemolytica.on July 4, 2020 by guest http://iai.asm.org/ Downloaded from bution of antibodies against this protein to complement-mediated killing of P. haemolytica. We found that the 45-kDa protein is a lipoprotein, designated PlpE, and that antibodies against PlpE, present in bovine immune sera, contribute to complement-mediated killing of P. haemolytica. MATERIALS AND METHODSBacteria, bacteriophage, culture media, and genomic library. P. haemolytica (89010807N) S1 was grown in BHI broth or on BHI agar (Difco Laboratories, Detroit, Mich.) as previously described (32). Escherichia coli BB4 and XL1-Blue and bacteriophages ZAPII and R408 were supplied with a P. haemolytica genomic DNA library (Clontech Laboratories, Palo Alto, Calif.) (37) and were grown according to the manufacturer's instructions. Recombinant E. coli strains were grown in the presence of ampicillin (50 g/ml).Bovine immune sera and purification of antibodies. Two bovine immune sera were used, one from a calf hyperimmunized with live P. haemolytica (25) and one from a calf that was vaccinated with P. haemolytica OMPs and was resistant to experimental P. haemolytica challenge (7). Briefly, the OMP-vaccinated calf was vaccinated subcutaneously on day 0 and day 21 with P. haemolytica S1 OMPs (2 mg in 1 ml of phosphate buffered saline [PBS] and 1 ml of an aluminum hydroxide-DDA-bromide adjuvant which has been described elsewhere in more detail [8]). On day 36, the calf was experimentally challenged transthoracically with 5 ml of a mixture containing 10 9 CFU of P. haemolytica S1/ml in each caudal lung lobe. Lung damage was evaluated upon necropsy 4 days after challenge, by using a previous...

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“…A further hindrance has been the lack of a transposon mutagenesis system for the organism; attempts using Tn5 and Tn10 have failed (44,Highlander,unpublished). These failures are likely the result of differences in gene expression between E. coli and M. haemolytica (209), though restriction by at least three restriction-modification systems in M. haemolytica also presents a significant barrier to gene transfer (210)(211)(212). As a result, it has been necessary to develop a genetic system for M. haemolytica using native plasmids and resistance genes.…”

Section: Systems For Genetic Manipulationmentioning

confidence: 99%

Molecular genetic analysis of virulence in Mannheimia (pasteurella) haemolytica

Highlander

2001

Front Biosci

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Mannheimia haemolytica (previously known as Pasteurella haemolytica) is a weakly hemolytic, gram-negative coccobacillus that is an opportunistic pathogen of cattle, sheep and other ruminants. In stressed, immunocompromised animals, the organism causes a fibrinous, necrotic pneumonia, commonly called "shipping fever". In the United States, economic losses due to shipping fever pneumonia surpass the combined cost of all other diseases of cattle. M. haemolytica, which is a member of the family Pasteurelleaceae, includes twelve serotypes (A1, A2, A5-A9, A12-14, A16 and A17) based on capsular antigen typing. Worldwide, serotypes A1 and A2 predominate, though all serotypes can cause disease. Serotype A1 causes pasteurellosis in cattle and has been the subject extensive study, while serotype A2 causes disease in sheep and is less-well characterized. Potential virulence factors of M. haemolytica have been identified and characterized by gene cloning and DNA sequence analysis. These factors include a ruminant-specific leukotoxin, an anti-phagocytic capsule, lipopolysaccharide, iron-regulated outer membrane proteins, lipoproteins, a sialoglycoprotease, a neuraminidase and two potential immunoglobulin proteases. Unlike the well-characterized leukotoxin, little is known about the expression of these other virulence factors. Attempts to dissect the mechanisms of M. haemolytica pathogenesis have been hindered by the lack of a robust genetic system for mutation of the organism, though new tools for genetic manipulation of M. haemolytica have been developed. Expression plasmids and operon fusion plasmids have been created and a series of antibiotic resistance cassettes useful for site-specific recombination have been constructed. It is anticipated that use of these tools for gene expression and mutagenesis, in combination with the soon to be released genomic sequence of a serotype A1 organism, will aid in understanding the molecular mechanisms of pathogenesis of M. haemolytica and will help to drive development of new vaccines to prevent shipping fever.

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An analysis of the codon usage of Pasteurella haemolytica A1

Cited by 3 publications

References 9 publications

Analysis of Genomic G + C Content, Codon Usage, Initiator Codon Context and Translation Termination Sites In Tetrahymena Thermophila

Analysis of Genomic G + C Content, Codon Usage, Initiator Codon Context and Translation Termination Sites In Tetrahymena Thermophila

Genetic and Immunologic Analyses of PlpE, a Lipoprotein Important in Complement-Mediated Killing ofPasteurella haemolyticaSerotype 1

Molecular genetic analysis of virulence in Mannheimia (pasteurella) haemolytica

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