Dataset Information

Gender-related secretome of Plasmodium berghei sexual stages

ABSTRACT: In this study, we applied a proteomic approach to identify proteins differentially released/secreted by female and male gametocytes of the rodent Plasmodium berghei activated to form gametes. We compared secreted molecules of the wild type gametocytes with those of a transgenic line defective in male gamete maturation and egress. This enabled us to provide a comprehensive dataset of egress-related molecules and their gender specificity. Using specific antibodies, we validated eleven candidate molecules, predicted as either gender-specific or common to both male and female gametocytes. All of them localize to punctuate, vesicle-like structures that relocate to cell periphery upon activation, but only three of them localize to the gametocyte-specific secretory vesicles named osmiophilic bodies. Our results confirm that the egress process involves a tightly coordinated secretory apparatus that includes different types of vesicles and may put the basis for functional studies aimed at designing novel transmission-blocking molecules.

INSTRUMENT(S): LTQ XL

ORGANISM(S): Plasmodium Berghei Anka (ncbitaxon:5823)

SUBMITTER: FEDERICA FRATINI

PROVIDER: MSV000084655 | MassIVE | Wed Dec 04 05:44:00 GMT 2019

SECONDARY ACCESSION(S): PXD016592

REPOSITORIES: MassIVE

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Identification and preliminary characterization of Plasmodium falciparum proteins secreted upon gamete formation.

Grasso Felicia F Fratini Federica F Albanese Tanino Giuseppe TG Mochi Stefania S Ciardo Mariagrazia M Pace Tomasino T Ponzi Marta M Pizzi Elisabetta E Olivieri Anna A

Scientific reports 20220610 1

Malaria long-term elimination depends on parasite transmission control. Plasmodium sexual stage maturation in the mosquito, including egress from the host erythrocyte, is one of the prime targets for transmission-blocking interventions. This work aims to identify candidate molecules potentially involved in gamete emergence from the host erythrocyte, as novel transmission blocking targets. We analyzed by quantitative mass spectrometry the proteins released/secreted by purified Plasmodium falcipar ...[more]

PMID: 35689013

Publication: 1/2

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