High Bacterial Agglutination Activity in a Single-CRD C-Type Lectin from Spodoptera exigua (Lepidoptera: Noctuidae)
Lectins are carbohydrate-interacting proteins that play a pivotal role in multiple physiological and developmental aspects of all organisms. They can specifically interact with different bacterial and viral pathogens through carbohydrate-recognition domains (CRD). In addition, lectins are also of bi...
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doaj-901eea5e20a446ff991a714ec62c34bc2020-11-24T23:29:34ZengMDPI AGBiosensors2079-63742017-03-01711210.3390/bios7010012bios7010012High Bacterial Agglutination Activity in a Single-CRD C-Type Lectin from Spodoptera exigua (Lepidoptera: Noctuidae)Leila Gasmi0Juan Ferré1Salvador Herrero2ERI de Biotecnología y Biomedicina (BIOTECMED), Department of Genetics, Universitat de València, 46100 Burjassot, SpainERI de Biotecnología y Biomedicina (BIOTECMED), Department of Genetics, Universitat de València, 46100 Burjassot, SpainERI de Biotecnología y Biomedicina (BIOTECMED), Department of Genetics, Universitat de València, 46100 Burjassot, SpainLectins are carbohydrate-interacting proteins that play a pivotal role in multiple physiological and developmental aspects of all organisms. They can specifically interact with different bacterial and viral pathogens through carbohydrate-recognition domains (CRD). In addition, lectins are also of biotechnological interest because of their potential use as biosensors for capturing and identifying bacterial species. In this work, three C-type lectins from the Lepidoptera Spodoptera exigua were produced as recombinant proteins and their bacterial agglutination properties were characterized. The lowest protein concentration producing bacterial agglutination against a panel of different Gram+ and Gram− as well as their carbohydrate binding specificities was determined for the three lectins. One of these lectins, BLL2, was able to agglutinate cells from a broad range of bacterial species at an extremely low concentration, becoming a very interesting protein to be used as a biosensor or for other biotechnological applications involving bacterial capture.http://www.mdpi.com/2079-6374/7/1/12C-type lectinagglutinationCRDbacterial detectionE. coli |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Leila Gasmi Juan Ferré Salvador Herrero |
spellingShingle |
Leila Gasmi Juan Ferré Salvador Herrero High Bacterial Agglutination Activity in a Single-CRD C-Type Lectin from Spodoptera exigua (Lepidoptera: Noctuidae) Biosensors C-type lectin agglutination CRD bacterial detection E. coli |
author_facet |
Leila Gasmi Juan Ferré Salvador Herrero |
author_sort |
Leila Gasmi |
title |
High Bacterial Agglutination Activity in a Single-CRD C-Type Lectin from Spodoptera exigua (Lepidoptera: Noctuidae) |
title_short |
High Bacterial Agglutination Activity in a Single-CRD C-Type Lectin from Spodoptera exigua (Lepidoptera: Noctuidae) |
title_full |
High Bacterial Agglutination Activity in a Single-CRD C-Type Lectin from Spodoptera exigua (Lepidoptera: Noctuidae) |
title_fullStr |
High Bacterial Agglutination Activity in a Single-CRD C-Type Lectin from Spodoptera exigua (Lepidoptera: Noctuidae) |
title_full_unstemmed |
High Bacterial Agglutination Activity in a Single-CRD C-Type Lectin from Spodoptera exigua (Lepidoptera: Noctuidae) |
title_sort |
high bacterial agglutination activity in a single-crd c-type lectin from spodoptera exigua (lepidoptera: noctuidae) |
publisher |
MDPI AG |
series |
Biosensors |
issn |
2079-6374 |
publishDate |
2017-03-01 |
description |
Lectins are carbohydrate-interacting proteins that play a pivotal role in multiple physiological and developmental aspects of all organisms. They can specifically interact with different bacterial and viral pathogens through carbohydrate-recognition domains (CRD). In addition, lectins are also of biotechnological interest because of their potential use as biosensors for capturing and identifying bacterial species. In this work, three C-type lectins from the Lepidoptera Spodoptera exigua were produced as recombinant proteins and their bacterial agglutination properties were characterized. The lowest protein concentration producing bacterial agglutination against a panel of different Gram+ and Gram− as well as their carbohydrate binding specificities was determined for the three lectins. One of these lectins, BLL2, was able to agglutinate cells from a broad range of bacterial species at an extremely low concentration, becoming a very interesting protein to be used as a biosensor or for other biotechnological applications involving bacterial capture. |
topic |
C-type lectin agglutination CRD bacterial detection E. coli |
url |
http://www.mdpi.com/2079-6374/7/1/12 |
work_keys_str_mv |
AT leilagasmi highbacterialagglutinationactivityinasinglecrdctypelectinfromspodopteraexigualepidopteranoctuidae AT juanferre highbacterialagglutinationactivityinasinglecrdctypelectinfromspodopteraexigualepidopteranoctuidae AT salvadorherrero highbacterialagglutinationactivityinasinglecrdctypelectinfromspodopteraexigualepidopteranoctuidae |
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1725545059611312128 |