ArticleInfection and immunity1991
Nucleotide sequence of the hemolysin I gene from Actinobacillus pleuropneumoniae.
Article in Infection and immunity, 1991. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 76 citations in OpenAlex.
- Type IV fimbrial subunit protein ApfA contributes to protection against porcine pleuropneumonia.Veterinary research · 2012Trial
- Review
- Inhibition of LtxA toxicity by blocking cholesterol binding with peptides.Molecular oral microbiology · 2016Article
- Differences in purinergic amplification of osmotic cell lysis by the pore-forming RTX toxins Bordetella pertussis CyaA and Actinobacillus pleuropneumoniae ApxIA: the role of pore size.Infection and immunity · 2013Article
- Acyltransferases in bacteria.Microbiology and molecular biology reviews : MMBR · 2013Review
- Review
- RTX proteins: a highly diverse family secreted by a common mechanism.FEMS microbiology reviews · 2010Review
- Identification, cloning, and expression of the CAMP-like factor autotransporter gene (cfa) of Bartonella henselae.Infection and immunity · 2005Article
- The N-terminal domain of RTX toxin ApxI of Actinobacillus pleuropneumoniae elicits protective immunity in mice.Infection and immunity · 2002Article
- Characterization of a predominant immunogenic outer membrane protein of Riemerella anatipestifer.Clinical and diagnostic laboratory immunology · 2000Article
- Characterization of PaxA and its operon: a cohemolytic RTX toxin determinant from pathogenic Pasteurella aerogenes.Infection and immunity · 2000Article
- Complete DNA sequence and detailed analysis of the Yersinia pestis KIM5 plasmid encoding murine toxin and capsular antigen.Infection and immunity · 1998Article
- Channel-forming activity and channel size of the RTX toxins ApxI, ApxII, and ApxIII of Actinobacillus pleuropneumoniae.Infection and immunity · 1996Article
- Analysis of the in vivo activation of hemolysin (HlyA) from Escherichia coli.Journal of bacteriology · 1996Article
- Characterization of an RTX toxin from enterohemorrhagic Escherichia coli O157:H7.Infection and immunity · 1996Article
- An Escherichia coli chromosomal ars operon homolog is functional in arsenic detoxification and is conserved in gram-negative bacteria.Journal of bacteriology · 1995Article
- Differential expression of the cytotoxic and hemolytic activities of the ApxIIA toxin from Actinobacillus pleuropneumoniae.Infection and immunity · 1994Article
- Transposon mutagenesis in Actinobacillus pleuropneumoniae with a Tn10 derivative.Journal of bacteriology · 1993Article
- Structural analysis of the Actinobacillus pleuropneumoniae-RTX-toxin I (ApxI) operon.Infection and immunity · 1993Article
- Molecular characterization of a leukotoxin gene from a Pasteurella haemolytica-like organism, encoding a new member of the RTX toxin family.Infection and immunity · 1993Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The DNA sequence of the gene encoding the structural protein of hemolysin I (HlyI) of Actinobacillus pleuropneumoniae serotype 1 strain 4074 was analyzed. The nucleotide sequence shows a 3,072-bp reading frame encoding a protein of 1,023 amino acids with a calculated molecular size of 110.1 kDa. This corresponds to the HlyI protein, which has an apparent molecular size on sodium dodecyl sulfate gels of 105 kDa. The structure of the protein derived from the DNA sequence shows three hydrophobic regions in the N-terminal part of the protein, 13 glycine-rich domains in the second half of the protein, and a hydrophilic C-terminal area, all of which are typical of the cytotoxins of the RTX (repeats in the structural toxin) toxin family. The derived amino acid sequence of HlyI shows 42% homology with the hemolysin of A. pleuropneumoniae serotype 5, 41% homology with the leukotoxin of Pasteurella haemolytica, and 56% homology with the Escherichia coli alpha-hemolysin. The 13 glycine-rich repeats and three hydrophobic areas of the HlyI sequence show more similarity to the E. coli alpha-hemolysin than to either the A. pleuropneumoniae serotype 5 hemolysin or the leukotoxin (while the last two are more similar to each other). Two types of RTX hemolysins therefore seem to be present in A. pleuropneumoniae, one (HlyI) resembling the alpha-hemolysin and a second more closely related to the leukotoxin. Ca(2+)-binding experiments using HlyI and recombinant A. pleuropneumoniae prohemolysin (HlyIA) that was produced in E. coli shows that HlyI binds 45Ca2+, probably because of the 13 glycine-rich repeated domains. Activation of the prohemolysin is not required for Ca2+ binding.
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