Heterogeneity in the attachment and uptake mechanisms of the Legionnaires' disease bacterium, Legionella pneumophila, by protozoan hosts

Article Abstract:

Investigation of the different mechanisms utilized for the attachment and uptake of Legionella pneumophila by both protozoa Hartmannella vermiformis and Acanthamoeba polyphaga was undertaken. Research reveals that the mechanisms of attachment and uptake of L. pneumophila by the two protozoan hosts are different. Uptake of the first is completely blocked by galactose and N-acetyl-D-galactosamine and only partially blocked A. polyphaga. Further evidence confirms the adaptivity of L. pneumophila to attach and invade different protozoan hosts.

Pathogenic microorganisms, Protozoans, Protozoa, Pathogenic

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Invasion of protozoa by Legionella pneumophila and its role in bacterial ecology and pathogenesis

Article Abstract:

The role of Legionella pneumophila in the bacterial ecology and pathogenesis of both mammals and protozoa has been widely documented since the outbreak of pneumonia in Jul 1976. Its ability to replicate and survive in the endosomal maturation-blocked phagosome is remarkable. The host-parasite interaction has been observed to be central to the ecology and pathogenesis of L. pneumophila whose infectious particle for Legionnaires' disease is an amoeba infected with the bacteria.

Causes of, Host-parasite relationships

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The type II secretion of Legionella pneumophila elaborates two aminopeptidases, as well as a metalloprotease that contributes to differential infection among protozoan hosts

Article Abstract:

The cloning of two proteins and the characterization of new mutants has shown that Legionella pneumophila has secreted aminopeptidases through its type II system. The analysis of aminopeptidases has shown that the type II-dependent ProA (MspA) metalloprotease has promoted Legionella pneumophila infection of Hartmannella vermiformis amoebae.

Science & research, Proteases, Mutation (Biology), Mutation, Chemical properties, Aminopeptidases

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