Identification and tissue-specific distribution of sulfated glycosaminoglycans in the blood-sucking bug Rhodnius prolixus (Linnaeus)

Costa-Filho, Adilson; Souza, Maisa L.S.; Martins, Rita C.L; Santos, André Vitor Fernandes dos; Silva, Gabriela V; Comarú, Michele Waltz; Moreira, Mônica F.; Atella, Geórgia C.; Allodi, Silvana; Nasciutti, Luiz Eurico; Masuda, Hatisaburo; Silva, Luiz‐Claudio F.

doi:10.1016/j.ibmb.2003.10.007

Cited by 9 publications

(16 citation statements)

References 28 publications

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“…3a, in bold). Unlike in mammals, for Drosophila (and putatively for other dipterans) the activity of a CS GalNAc-transferase I (GalNAcT-I) as opposed to an N-acetylglucosaminyl transferase I (GlcNAcT-I) determine the initiation and progression of the chain toward either a CSGAG or HSGAG, respectively (16)(17)(18) (Fig. 3a).…”

Section: The Anopheles Gambiae Gag Biosynthetic Pathway and Cloning Omentioning

confidence: 99%

Plasmodium falciparum ookinetes require mosquito midgut chondroitin sulfate proteoglycans for cell invasion

Dinglasan

Alaganan

Ghosh

et al. 2007

Proc. Natl. Acad. Sci. U.S.A.

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Malaria transmission entails development of the Plasmodium parasite in its insect vector, the Anopheles mosquito. Parasite invasion of the mosquito midgut is the critical first step and involves adhesion to host epithelial cell ligands. Partial evidence suggests that midgut oligosaccharides are important ligands for parasite adhesion; however, the identity of these glycans remains unknown. We have identified a population of chondroitin glycosaminoglycans along the apical midgut microvilli of Anopheles gambiae and further demonstrated ookinete recognition of these glycans in vitro. By repressing the expression of the peptide-Oxylosyltransferase homolog of An. gambiae by means of RNA interference, we blocked glycosaminoglycan chain biosynthesis, diminished chondroitin sulfate levels in the adult midgut, and substantially inhibited parasite development. We provide evidence for the in vivo role of chondroitin sulfate proteoglycans in Plasmodium falciparum invasion of the midgut and insight into the molecular mechanisms mediating parasite-mosquito interactions.Anopheles ͉ glycosaminoglycans ͉ glycosytransferase ͉ malaria ͉ RNAi M alaria is caused by Plasmodium parasites, among which, Plasmodium falciparum inflicts the severest infection on human populations. The complex parasite life cycle includes developmental stages within both mammals and its obligatory insect vector, the Anopheles mosquito (1). Plasmodium gametocytes that are taken up in an infected blood meal transform into ookinetes in the mosquito midgut lumen. Ookinetes then migrate to the gut periphery where they are thought to recognize and adhere to midgut ligands. These steps directly precede cell invasion, traversal, and the differentiation of ookinetes into oocysts beneath the basal lamina. Each oocyst produces thousands of sporozoites that subsequently invade the mosquito salivary glands and are delivered to a vertebrate host during a succeeding blood meal. Clearly, ookinete invasion of midgut epithelia is the critical step for parasite establishment in the mosquito and, therefore, represents the best paradigm to develop novel transmission-blocking strategies (i.e., approaches that prevent parasite passage through the mosquito and therefore impede the subsequent cascade of secondary infections in humans).Plasmodium ookinete molecules belonging to the Thrombospondin-related adhesive protein (TRAP) family, which includes the sporozoite surface protein, TRAP, and two ookinete proteins, the circumsporozoite and TRAP-related protein (CTRP) and the von Willebrand Factor A domain protein (WARP), have been demonstrated to bind to the glycosaminoglycan (GAG), heparin, in vitro (2). The major circumsporozoite protein (CSP) and TRAP both recognize heparan sulfate (HS) proteoglycans on the liver sinusoid, a critical step toward the establishment of parasite infection in humans (3, 4). Similarly, ookinete CTRP and WARP gene knockouts were shown to be incapable of invading the mosquito midgut, strongly implying their essential role in mosquito midgut cell invasion ...

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Section: The Anopheles Gambiae Gag Biosynthetic Pathway and Cloning Omentioning

confidence: 99%

Plasmodium falciparum ookinetes require mosquito midgut chondroitin sulfate proteoglycans for cell invasion

Dinglasan

Alaganan

Ghosh

et al. 2007

Proc. Natl. Acad. Sci. U.S.A.

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“…Sulfated GAGs were isolated from cockroach tissues following a previously described method for the isolation of these molecules from triatomines (Costa-Filho et al, 2004). Briefly, dried tissues or a suspension containing the fat bodies were suspended or mixed in sodium acetate buffer, pH 5.5, containing 40 mg papain in the presence of 5 mM EDTA and 5 mM cysteine at 60 8C for 24 h. The suspension was centrifuged at 2000!g for 10 min at room temperature and the supernatant, which contained the GAGs, was then applied to a Mono Q-FPLC column, equilibrated with 20 mM Tris-HCl (pH 8.0).…”

Section: Isolation Of Sulfated Gags From Dissected Tissuesmentioning

confidence: 99%

“…Briefly, dried tissues or a suspension containing the fat bodies were suspended or mixed in sodium acetate buffer, pH 5.5, containing 40 mg papain in the presence of 5 mM EDTA and 5 mM cysteine at 60 8C for 24 h. The suspension was centrifuged at 2000!g for 10 min at room temperature and the supernatant, which contained the GAGs, was then applied to a Mono Q-FPLC column, equilibrated with 20 mM Tris-HCl (pH 8.0). The column was washed with 20 mL of the same buffer and then eluted step-wise with 20 mL of 0.6 M NaCl, to remove sulfated contaminants (Costa-Filho et al, 2004), and the bound sulfated GAGs were eluted with 20 mL of 2.0 M NaCl in the same acetate buffer. The sulfated GAGs eluted from the column were exhaustively dialyzed against distilled water, lyophilized and dissolved in 0.1 mL of distilled water.…”

Section: Isolation Of Sulfated Gags From Dissected Tissuesmentioning

confidence: 99%

“…Purified cockroach sulfated GAGs were characterized by agarose gel electrophoresis and deaminative cleavage with nitrous acid (Costa-Filho et al, 2004), as described below.…”

Section: Characterization Of the Sulfated Gagsmentioning

confidence: 99%

“…Nitrous acid depolymerization of the sulfated GAGsThe presence of HS was confirmed by destroying this GAG by deaminating the sample with nitrous acid at pH 1.5 as described by Costa-Filho et al (2004). Briefly, approximately 10 mg of cockroach sulfated GAGs were incubated with 20 mL of fresh generated nitrous acid at room temperature for 90 min.…”

Section: Characterization Of the Sulfated Gagsmentioning

confidence: 99%

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