Lectin-binding sites in the midgut of the mosquitoesAnopheles stephensi Liston andAedes aegypti L. (Diptera: Culicidae)

Rudin, W.; Hecker, Hermann

doi:10.1007/bf00931811

Cited by 86 publications

(48 citation statements)

References 24 publications

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“…As the parasite was seen in ultrastructural studies to disrupt the membrane (3), the biochemical basis of penetration would depend on the chemical composition of the membrane. The peritrophic membrane had been suggested, from indirect studies, to consist of chitin (9). The demonstration in the present study of the release of N-acetylglucosamine by the action of chitinase provides direct evidence for the presence of chitin in A. agypti peritrophic membrane.…”

Section: Discussionsupporting

confidence: 59%

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Malaria parasite chitinase and penetration of the mosquito peritrophic membrane.

Huber

Cabib

Miller

1991

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

192

116

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Malaria parasites (ookinetes) appear to digest the peritrophic membrane in the mosquito midgut during penetration. Previous studies demonstrated that lectins specific for N-acetylglucosamine bind to the peritrophic membrane and proposed that the membrane contains chitin [Rudin, W. & Hecker, H. (1989) Parasitol. Res. 75, 268-2791 In the present study, we show that the peritrophic membrane is digested by Serratia marcescens chitinase (EC 3.2.1.14), leading to the release of N-acetylglucosamine and fragmentation of the membrane. We also report the presence of a malaria parasite chitinase that digests 4-methylumbelliferyl chitotriose. The enzyme is not detectable until 15 hr after zygote formation, the time required for maturation of the parasite from a zygote to an ookinete, the invasive form of the parasite. At 20 hr, the enzyme begins to appear in the culture supernatant. The chitinase extracted from the parasite and found in the culture supernatant consists of a major band and two minor bands of activity on native polyacrylamide gel electrophoresis. The presence of chitin in the peritrophic membrane, the disruption of the peritrophic membrane during invasion, and the presence of chitinase in ookinetes suggest that the chitinase in ookinetes is used in the penetration of the peritrophic membrane.The peritrophic membrane found in the midgut of arthropods is defined as a membranous sac surrounding the ingested blood (1). The function of the peritrophic membrane in the various arthropod orders is unclear, but there is speculation that in bloodsucking insects it is one of the factors determining the competence for the transmission of parasites (2,3). These insects form a peritrophic membrane in response to the mechanical distention resulting from the uptake of blood (4). In Aedes aegypti, formation starts immediately after the blood meal, but about 12 hr elapse before it attains a mature structure (5, 6). Plasmodium gallinaceum, an avian malaria parasite that infects A. aegypti, develops motile ookinetes in the blood meal in 16-20 hr (3, 7). Parasites begin to appear in the midgut epithelial cells around 24 hr, but the major invasion occurs around 30 hr (3). As the peritrophic membrane is fully formed in 12 hr and does not dissolve until 48 hr after the blood meal, the parasite must traverse the peritrophic membrane to move from the blood meal to the epithelial cells. A recent ultrastructural study (3) produced direct evidence that the peritrophic membrane is a barrier to infection. The peritrophic membrane surrounding the penetrating ookinetes lost its laminated structure and was less electron dense. Electron-dense material extended from the anterior end of the parasite. A similar modification was previously observed with Babesia microti passing through the peritrophic membrane of Ixodes ticks (8). Because evidence has been presented that the peritrophic membrane contains chitin (9), we searched for chitinase activity in the parasite that might be used to cross the peritrophic membrane. We report here that P...

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Section: Discussionsupporting

confidence: 59%

“…Previous studies demonstrated that lectins specific for N-acetylglucosamine bind to the peritrophic membrane and proposed that the membrane contains chitin [Rudin, W. & Hecker, H. (1989) Parasitol. Res.…”

mentioning

confidence: 99%

Malaria parasite chitinase and penetration of the mosquito peritrophic membrane.

Huber

Cabib

Miller

1991

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

192

116

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“…Consequently, the arthropod midgut serves as both barrier and gateway to pathogen invasion (97,107). The luminal face of the midgut epithelium is covered by a dense array of glycoconjugates that may act as a "glycan receptor-buffet" for a myriad of pathogens (107).…”

Section: The Midgut: the Principal Pathogen Gatewaymentioning

confidence: 99%

Insight into a Conserved Lifestyle: Protein-Carbohydrate Adhesion Strategies of Vector-Borne Pathogens

Dinglasan

Jacobs-Lorena

2005

Infect Immun

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The incidence of vector-borne diseases such as malaria, dengue, African sleeping sickness, and tick-borne fevers is increasing. Given that current global control efforts have met with limited success, the need to develop novel interventions has become all the more vital. Successful discovery of such interventions is contingent on improving our understanding of how the pathogen interacts with its vertebrate host and also with its invertebrate vector. In this review we examine a premise developed more than 20 years ago (94) that emphasized the role of protein-carbohydrate interactions in microbial pathogenesis, and we present it in the context of vector-pathogen dynamics.Glycans are "essential macromolecules for numerous cellular processes, such as signaling, structural-support, cell-cell interaction, cell-matrix adhesion, growth, protection and trafficking" (94). Their ubiquitous yet tissue-specific occurrence as cell surface glycoconjugates has, over evolutionary time, been exploited by several pathogenic microorganisms as receptors for attachment and invasion (95). While evidence for microbial adherence to mammalian glycolipids and glycoproteins continues to grow (for reviews see references 17, 18, 58, 95, and 115), only recently has evidence for a "protein-carbohydrate recognition strategy" for vector host-pathogen interactions emerged. This review focuses on the most recent advances that describe adherence mechanisms of three different classes of pathogens-bacteria, viruses, and protozoan parasites-to their obligate arthropod vectors. We also discuss how the proteincarbohydrate recognition strategies in both vector and mammalian life stages are apparently conserved and how this conservation could lead to the development of novel strategies for intervention.

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“…Another protective structure is the glycocalyx (glyco ϭ sweet͞sugar, calyx ϭ shell), which is an integral part of the microvillar membrane and appears as an electron-dense fuzzy coat on the outside of the microvillar surface (4,10). The glycocalyx, including that of mosquitoes, is rich in carbohydrates, as it is recognized by a variety of lectins (11,12). However, no experimental data are currently available on the molecular composition of the insect midgut glycocalyx.…”

mentioning

confidence: 99%

A cell surface mucin specifically expressed in the midgut of the malaria mosquito Anopheles gambiae

Shen

Dimopoulos

Kafatos

et al. 1999

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

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An invertebrate intestinal mucin gene, AgMuc1, was isolated from the malaria vector mosquito Anopheles gambiae. The predicted 122-residue protein consists of a central core of seven repeating TTTTVAP motifs f lanked by hydrophobic N-and C-terminal domains. This structure is similar to that of mucins that coat the protozoan parasite Trypanosoma cruzi. Northern blot analysis indicated that the gene is expressed exclusively in the midgut of adult mosquitoes. A length polymorphism and in situ hybridization were used to genetically and cytogenetically map AgMuc1 to division 7A of the right arm of the second chromosome. The subcellular localization of the encoded protein in tissue culture cells was examined by using a baculovirus vector to express AgMuc1 protein tagged with the green f luorescent protein (GFP). The results indicated that this protein is found at the cell surface and that both hydrophobic domains are required for cell surface targeting. We propose that AgMuc1 is an abundant mucin-like protein that lines the surface of the midgut microvilli, potentially protecting the intestinal epithelium from the proteinase-rich environment of the gut lumen. An intriguing possibility is that, as an abundant surface protein, AgMuc1 may also interact with the malaria parasite during its invasion of the mosquito midgut.

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Lectin-binding sites in the midgut of the mosquitoesAnopheles stephensi Liston andAedes aegypti L. (Diptera: Culicidae)

Cited by 86 publications

References 24 publications

Malaria parasite chitinase and penetration of the mosquito peritrophic membrane.

Malaria parasite chitinase and penetration of the mosquito peritrophic membrane.

Insight into a Conserved Lifestyle: Protein-Carbohydrate Adhesion Strategies of Vector-Borne Pathogens

A cell surface mucin specifically expressed in the midgut of the malaria mosquito Anopheles gambiae

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