2000
DOI: 10.1046/j.1365-2583.2000.00202.x
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Molecular cloning and characterization of a metal responsive Aedes aegypti intestinal mucin cDNA

Abstract: We have isolated a cDNA from Aedes aegypti that is transcribed in the larval midgut in response to metal exposure, and in the adult female midgut in response to iron or cadmium exposure, or a blood meal. The cDNA encodes a protein, designated Aedes aegypti intestinal mucin 1 (AEIMUC1), which has similarities with invertebrate intestinal mucins and peritrophins, and vertebrate mucins. Proline, serine and threonine comprise 30% of the amino acid composition of AEIMUC1, a characteristic of mucins. AEIMUC1 contain… Show more

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Cited by 43 publications
(53 citation statements)
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“…AEIMUC1 exhibits similarity to these and other insect midgut proteins (10). The overall organization of the CRDs and the PTSB of our AEIMUC1 most closely resembles that of the moth larval intestinal mucin.…”
Section: Aedes Aegypti: Anatomic Basis Of Heavy-metal Toxicity To Larvaementioning
confidence: 58%
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“…AEIMUC1 exhibits similarity to these and other insect midgut proteins (10). The overall organization of the CRDs and the PTSB of our AEIMUC1 most closely resembles that of the moth larval intestinal mucin.…”
Section: Aedes Aegypti: Anatomic Basis Of Heavy-metal Toxicity To Larvaementioning
confidence: 58%
“…The fact that AEIMUC1 is induced by virus infection tends to support this hypothesis. Mucins are well known for their ability to bind pathogens such as viruses and bacteria, thereby inhibiting infection (10,21,(27)(28)(29)(30)(31). To overcome the mucin blockade, numerous pathogens have developed specific mucin-degrading enzymes (29,(34)(35)(36).…”
Section: Aedes Aegypti: Anatomic Basis Of Heavy-metal Toxicity To Larvaementioning
confidence: 99%
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“…It was remarkable to find homology with a set of mostly unknown insect proteins, all sharing the same consensus sequence of 37-41 residues. One of these homologues is a putative salivary secreted mucin 3 from Aedes aegypti, but as icarapin has no regions rich in proline, threonine and serine residues occurring in clusters (in spite of its high Pro, Thr, Ser content of 21%) and cysteine residues are absent, it lacks some common features of mucins or mucin-like proteins [12].…”
Section: Discussionmentioning
confidence: 99%