title: The Interactions of Allium sativum leaf agglutinin with a chaperonin group of unique receptor protein isolated from a bacterial endosymbiont of the mustard aphid.
abstract: The homopteran sucking insect, Lipaphis erysimi (mustard aphid) causes severe damage to various crops. This pest not only affects plants by sucking on the phloem, but it also transmits single-stranded RNA luteoviruses while feeding, which cause disease and damage in the crop. The mannose-binding Allium sativum (garlic) leaf lectin has been found to be a potent control agent of L. erysimi. The lectin receptor protein isolated from brush border membrane vesicle of insect gut was purified to determine the mechanism of lectin binding to the gut. Purified receptor was identified as an endosymbiotic chaperonin, symbionin, using liquid chromatography-tandem mass spectrometry. Symbionin from endosymbionts of other aphid species have been reported to play a significant role in virus transmission by binding to the read-through domain of the viral coat protein. To understand the molecular interactions of the said lectin and this unique symbionin molecule, the model structures of both molecules were generated using the Modeller program. The interaction was confirmed through docking of the two molecules forming a complex. A surface accessibility test of these molecules demonstrated a significant reduction in the accessibility of the complex molecule compared with that of the free symbionin molecule. This reduction in surface accessibility may have an effect on other molecular interactive processes, including "symbionin virion recognition", which is essential for such symbionin-mediated virus transmission. Thus, garlic leaf lectin provides an important component of a crop management program by controlling, on one hand, aphid attack and on the other hand, symbionin-mediated luteovirus transmission.
authors.affiliation: Plant Molecular and Cellular Genetics, Bose Institute, P-1/12, C.I.T. Scheme, VII-M, Calcutta 700054, India.
authors.forename: Santanu
authors.initials: S
authors.lastname: Banerjee
authors.forename: Daniel
authors.initials: D
authors.lastname: Hess
authors.forename: Pralay
authors.initials: P
authors.lastname: Majumder
authors.forename: Debjani
authors.initials: D
authors.lastname: Roy
authors.forename: Sampa
authors.initials: S
authors.lastname: Das
mesh_terms: D000373:Agglutinins / Q000378:metabolism*; D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D018833:Chaperonins / Q000235:genetics / Q000378:metabolism; D005737:Garlic / Q000378:metabolism*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009149:Mustard Plant / Q000382:microbiology; D011485:Protein Binding; D011956:Receptors, Cell Surface / Q000235:genetics / Q000378:metabolism; D013559:Symbiosis
chemical_list: D000373:Agglutinins; D001426:Bacterial Proteins; D011956:Receptors, Cell Surface; D018833:Chaperonins