Essential Domains of Invasins Utilized to Infect Mammalian Host Cells
Anaplasma phagocytophilum causes the potentially deadly bacterial disease granulocytic anaplasmosis. The pathogen replicates inside white blood cells and, like all other obligate intracellular organisms, must enter host cells to survive. Multiple A. phagocytophilum surface proteins called invasins cooperatively orchestrate the entry process. Identifying these proteins’ domains that are required for function, and determining the molecular basis of their interaction with host cell receptors would significantly advance understanding of A. phagocytophilum pathogenesis. In this study, the binding domains of two A. phagocytophilum surface proteins, OmpA and Asp14, were identified. The specific OmpA residues that interact with its host cell receptor were also defined. An antibody cocktail generated against the binding domains of OmpA, Asp14, and a third invasin, AipA, blocked the ability of A. phagocytophilum to infect host cells. The data presented within suggest that binding domains of OmpA, Asp14, and AipA could be exploited to develop a vaccine for granulocytic anaplasmosis.
Vyšlo v časopise:
Essential Domains of Invasins Utilized to Infect Mammalian Host Cells. PLoS Pathog 11(2): e32767. doi:10.1371/journal.ppat.1004669
Kategorie:
Research Article
prolekare.web.journal.doi_sk:
https://doi.org/10.1371/journal.ppat.1004669
Souhrn
Anaplasma phagocytophilum causes the potentially deadly bacterial disease granulocytic anaplasmosis. The pathogen replicates inside white blood cells and, like all other obligate intracellular organisms, must enter host cells to survive. Multiple A. phagocytophilum surface proteins called invasins cooperatively orchestrate the entry process. Identifying these proteins’ domains that are required for function, and determining the molecular basis of their interaction with host cell receptors would significantly advance understanding of A. phagocytophilum pathogenesis. In this study, the binding domains of two A. phagocytophilum surface proteins, OmpA and Asp14, were identified. The specific OmpA residues that interact with its host cell receptor were also defined. An antibody cocktail generated against the binding domains of OmpA, Asp14, and a third invasin, AipA, blocked the ability of A. phagocytophilum to infect host cells. The data presented within suggest that binding domains of OmpA, Asp14, and AipA could be exploited to develop a vaccine for granulocytic anaplasmosis.
Zdroje
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Štítky
Hygiena a epidemiológia Infekčné lekárstvo LaboratóriumČlánok vyšiel v časopise
PLOS Pathogens
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