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Type II protein secretion (T2S) byLegionella pneumophila is required for intracellular infection of host cells, including macrophages and the amoebaeAcanthamoeba castellanii andHartmannella vermiformis . Previous proteomic analysis revealed that T2S byL. pneumophila 130b mediates the export of &gt;25 proteins, including several that appeared to be novel. Following confirmation that they are unlike known proteins, T2S substrates NttA, NttB, and LegP were targeted for mutation.nttA mutants were impaired for intracellular multiplication inA. castellanii but notH. vermiformis or macrophages, suggesting that novel exoproteins which are specific toLegionella are especially important for infection. Because the importance of NttA was host cell dependent, we examined a panel of T2S substrate mutants that had not been tested before in more than one amoeba. As a result, RNase SrnA, acyltransferase PlaC, and metalloprotease ProA all proved to be required for optimal intracellular multiplication inH. vermiformis but notA. castellanii . Further examination of anlspF mutant lacking the T2S apparatus documented that T2S is also critical for infection of the amoebaNaegleria lovaniensis . Mutants lacking SrnA, PlaC, or ProA, but not those deficient for NttA, were defective inN. lovaniensis . Based upon analysis of a double mutant lacking PlaC and ProA, the role of ProA inH. vermiformis was connected to its ability to activate PlaC, whereas inN. lovaniensis , ProA appeared to have multiple functions. Together, these data document that the T2S system exports multiple effectors, including a novel one, which contribute in different ways to the broad host range ofL. pneumophila .

infection and immunity

Multiple Legionella pneumophila Type II Secretion Substrates, Including a Novel Protein, Contribute to Differential Infection of the Amoebae Acanthamoeba castellanii, Hartmannella vermiformis, and Naegleria lovaniensis