Glycosylation in malaria parasites: what do we know?

Gowda, D. Channe; Miller, Louis H.

doi:10.1016/j.pt.2023.12.006

Cited by 7 publications

(5 citation statements)

References 93 publications

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“…pastoris may lead to low product yield. Another unwanted feature of the yeast system is the glycosylation of expressed proteins, which may interfere with their antigenicity, since Plasmodium proteins are typically not glycosylated [ 35 ].…”

Section: Discussionmentioning

confidence: 99%

Evaluation of transmission-blocking potential of PvPSOP25 using transgenic murine malaria parasite and clinical isolates

Zhang,

Feng,

Zhao

et al. 2024

PLoS Negl Trop Dis

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Background Malaria transmission-blocking vaccines (TBVs) aim to inhibit malaria parasite development in mosquitoes and prevent further transmission to the human host. The putative-secreted ookinete protein 25 (PSOP25), highly conserved in Plasmodium spp., is a promising TBV target. Here, we investigated PvPSOP25 from P. vivax as a TBV candidate using transgenic murine parasite P. berghei and clinical P. vivax isolates. Methods and findings A transgenic P. berghei line expressing PvPSOP25 (TrPvPSOP25Pb) was generated. Full-length PvPSOP25 was expressed in the yeast Pichia pastoris and used to immunize mice to obtain anti-rPvPSOP25 sera. The transmission-blocking activity of the anti-rPvPSOP25 sera was evaluated through in vitro assays and mosquito-feeding experiments. The antisera generated by immunization with rPvPSOP25 specifically recognized the native PvPSOP25 antigen expressed in TrPvPSOP25Pb ookinetes. In vitro assays showed that the immune sera significantly inhibited exflagellation and ookinete formation of the TrPvPSOP25Pb parasite. Mosquitoes feeding on mice infected with the transgenic parasite and passively transferred with the anti-rPvPSOP25 sera showed a 70.7% reduction in oocyst density compared to the control group. In a direct membrane feeding assay conducted with five clinical P. vivax isolates, the mouse anti-rPvPSOP25 antibodies significantly reduced the oocyst density while showing a negligible influence on mosquito infection prevalence. Conclusions This study supported the feasibility of transgenic murine malaria parasites expressing P. vivax antigens as a useful tool for evaluating P. vivax TBV candidates. Meanwhile, the moderate transmission-reducing activity of the generated anti-rPvPSOP25 sera necessitates further research to optimize its efficacy.

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Section: Discussionmentioning

confidence: 99%

Evaluation of transmission-blocking potential of PvPSOP25 using transgenic murine malaria parasite and clinical isolates

Zhang,

Feng,

Zhao

et al. 2024

PLoS Negl Trop Dis

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“…stephensi SG proteins because it was present at levels below the threshold of detection in the lectin microarrays or because α-gal is possibly present only in mosquito glycolipids [21] which were not investigated in the present study. The previously reported detection of α-gal in Plasmodium sporozoites and SGs of anopheline vectors [7] may be caused by the non-specific GSI-B4 binding documented previously [8] and monoclonal antibody cross-reactivity, but requires further investigation because of its important implications for immunity against malaria [6][7][8][9][10].…”

Section: Discussionmentioning

confidence: 99%

“…The presence of α-gal on the surfaces of mosquito SG-derived sporozoite stages of human and rodent malaria parasites (Plasmodium falciparum and Plasmodium yoelii/berghei respectively) was reported from the binding of Griffonia simplicifolia-I isolectin B4 (GSI-B4) and a monoclonal antibody against α-gal [7]. The absence of genes for galactosyl transferases in the Plasmodium genome [6,8], the absence of significant Golgi glycosylation [9], the failure to incorporate galactose from UDP-gal into glycolipids and glycoproteins in cultured asexual blood stages, and the non-specific binding of GSI-B4 to P. falciparum [8], raised the alternate possibility that Plasmodium sporozoites may have acquired α-gal containing glycoconjugates from the SGs of Anopheles mosquito vectors [6,10]. Dengue virus replicating in the arboviral mosquito vector Aedes albopictus derived C6/36 cell line reportedly acquired α-gal on virus envelope N-glycans based on lectin binding and MS analysis [11].…”

Section: Introductionmentioning

confidence: 99%

Lectin Microarray Analysis of Salivary Gland Glycoproteins from the Arboviral VectorAedes aegyptiand the Malaria VectorAnopheles stephensi

Ramasamy,

Chen,

Zhang

et al. 2024

Preprint

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Salivary gland glycoconjugates in human-feeding insects and arachnids can elicit hypersensitivity reactions. Glycoproteins introduced during blood feeding by arachnid ticks are responsible for red meat allergy or the α-gal syndrome. Dengue virus transmitted byAedesmosquitoes incorporates mosquito glycoproteins into its envelope and malaria parasites transmitted byAnophelesmosquitoes reportedly express α-gal epitopes that are potentially derived from mosquito salivary glands. Tick salivary gland glycoproteins possess α-gal epitopes. We used microarrays containing forty different lectins to analyse salivary gland protein glycoconjugates from the principal arboviral vectorAedes aegyptiand the rapidly spreading malaria vectorAnopheles stephensi. Salivary gland glycoproteins of both mosquitoes possessed very similar lectin-binding specificities. Lectin-binding profiles showed the significant presence of oligomannose N-glycans and O-glycans, a limited presence of glycan structures capped with terminal GalNAc, GlcNAc, β linked Gal, α1-6 linked fucose, and no detectable sialic acids or terminal α-linked Gal in salivary gland glycoproteins.

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“…Glycosylation started to be intensively studied in Plasmodium in the 80s-90s when the importance of N-linked glycoproteins for P.f. development in the erythrocyte was suggested [ 154 , 155 ]. Protein O- and C-glycosylation were initially highly discussed and doubted for Plasmodium , while well characterized for Toxoplasma [ 156 , 157 ].…”

Section: Protein Ptms In Plasmodium Parasite Growt...mentioning

confidence: 99%

Post-Translational Modifications of Proteins of Malaria Parasites during the Life Cycle

Schwarzer,

Skorokhod

2024

IJMS

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Post-translational modifications (PTMs) are essential for regulating protein functions, influencing various fundamental processes in eukaryotes. These include, but are not limited to, cell signaling, protein trafficking, the epigenetic control of gene expression, and control of the cell cycle, as well as cell proliferation, differentiation, and interactions between cells. In this review, we discuss protein PTMs that play a key role in the malaria parasite biology and its pathogenesis. Phosphorylation, acetylation, methylation, lipidation and lipoxidation, glycosylation, ubiquitination and sumoylation, nitrosylation and glutathionylation, all of which occur in malarial parasites, are reviewed. We provide information regarding the biological significance of these modifications along all phases of the complex life cycle of Plasmodium spp. Importantly, not only the parasite, but also the host and vector protein PTMs are often crucial for parasite growth and development. In addition to metabolic regulations, protein PTMs can result in epitopes that are able to elicit both innate and adaptive immune responses of the host or vector. We discuss some existing and prospective results from antimalarial drug discovery trials that target various PTM-related processes in the parasite or host.

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Glycosylation in malaria parasites: what do we know?

Cited by 7 publications

References 93 publications

Evaluation of transmission-blocking potential of PvPSOP25 using transgenic murine malaria parasite and clinical isolates

Evaluation of transmission-blocking potential of PvPSOP25 using transgenic murine malaria parasite and clinical isolates

Lectin Microarray Analysis of Salivary Gland Glycoproteins from the Arboviral VectorAedes aegyptiand the Malaria VectorAnopheles stephensi

Post-Translational Modifications of Proteins of Malaria Parasites during the Life Cycle

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