Monsicha Pongpom, Pritsana Sawatdeechaikul and Nongnuch Vanittanakom*

Department of Microbiology, Faculty of Medicine, Chiang Mai University, Thailand

*Corresponding Author: Nongnuch Vanittanakom, Department of Microbiology, Faculty of Medicine, Chiang Mai University, Muang, Chiang Mai, Thailand.

Received: December 20, 2017; Published: February 06, 2018

DOI: 10.31080/ASMI.2018.01.0022

Citation: Nongnuch Vanittanakom., et al. “An Antigenic Protein Mplp6 is Dispensable in Talaromyces marneffei ”. Acta Scientific Microbiology 1.3 (2018).

Abstract

  MPLP6 is one of the genes in the mannoprotein superfamily of a human pathogenic fungus Talaromyces marneffei . It encodes for a highly immunogenic, yeast phase specific protein Mplp6. In this study, to analyze the function of MPLP6 , the deletion and re- constitution strains were constructed and characterized phenotypically. The mutant strain demonstrated the same phenotypes as those of the wild type isolate; the morphology of the colony, growth rate and conidiation, indicating the dispensability of the MPLP6 gene. Growth of the mutant on fatty acid containing media was similar to that observed in the wild type, implying that Mplp6 is not required for fatty acid utilization. Moreover, the mutant showed cell wall, hyper-osmotic and oxidative stress tolerance similar to the wild type; therefore it is reasonable to conclude that Mplp6 is not the component that takes responsibility in cell wall integrity. In addition, the mutant was phagocytosed and killed in equal measures when compared with the wild type and complementary strains when observed in the THP-1 monocyte-derived macrophage infection model. Interestingly, attachment of the yeast cells of the mutant to fibronectin and laminin was slightly reduced when compared to the parental strain, suggesting that the Mplp6 could serve as one of the molecules that contribute to the host-pathogen interaction. Additionally, the recombinant Mplp6 could bind to both extracellular matrix molecules in a dose-dependent manner. These results suggest that the Mplp6 could be a putative adhesin.

Keywords: MPLP6 ; Mplp6; Mannoprotein; Function; Talaromyces marneffei

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