Glycosylation on proteins of the intestine and perimicrovillar membrane of Triatoma (Meccus) pallidipennis, under different feeding conditions

Trypanosoma cruzi, the causative agent of Chagas disease, interacts with molecules in the midgut of its insect vector to multiply and reach the infective stage. Many studies suggest that the parasite binds to midgut‐specific glycans. We identified several glycoproteins expressed in the intestine and...

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Published inInsect science Vol. 26; no. 5; pp. 796 - 808
Main Authors Gutiérrez‐Cabrera, Ana E., Zandberg, Wesley F., Zenteno, Edgar, Rodríguez, Mario H., Espinoza, Bertha, Lowenberger, Carl
Format Journal Article
LanguageEnglish
Published Australia Wiley Subscription Services, Inc 01.10.2019
Subjects
Antibodies
Chagas' disease
Epitopes
Feeding
feeding conditions
Glycoproteins
Glycosylation
Infective stages
Insects
Intestine
Lectins
Mannose
Midgut
perimicrovillar membrane
Polysaccharides
Proteins
Sugar
Triatoma
triatomine
Vector-borne diseases
vector–parasite interactions
perimicrovillar membrane
glycoproteins
feeding conditions
vector-parasite interactions
triatomine
lectins
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Summary:Trypanosoma cruzi, the causative agent of Chagas disease, interacts with molecules in the midgut of its insect vector to multiply and reach the infective stage. Many studies suggest that the parasite binds to midgut‐specific glycans. We identified several glycoproteins expressed in the intestine and perimicrovillar membrane (PMM) of Triatoma (Meccus) pallidipennis under different feeding conditions. In order to assess changes in protein‐linked glycans, we performed lectin and immunoblot analyses on glycoprotein extracts from these intestinal tissues using well‐characterized lectins, and an antibody, which collectively recognize a wide range of different glycans epitopes. We observed that the amount and composition of proteins and glycoproteins associated with different glycans structures changed over time in the intestines and PMM under different physiological conditions. PMM extracts contained a wide variety of glycoproteins with different sugar residues, including abundant high‐mannose and complex sialylated glycans. We propose that these molecules could be involved in the process of parasite–vector interactions.
Bibliography:These authors contributed equally to this work and both should be considered first authors.
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ISSN:1672-9609
1744-7917
DOI:10.1111/1744-7917.12579