BibTex format
@article{Benjamin:2024:10.1016/j.jbc.2024.107869,
author = {Benjamin, S and Jégouzo, S and Lieng, C and Daniels, C and Coispeau, M and Lau, R and Kim, S and Metaxa, Y and Philpott, J and Li, T and Dai, C and Wang, X and Newby, M and Pier, G and Crispin, M and Clements, A and Taylor, M and Drickamer, K},
doi = {10.1016/j.jbc.2024.107869},
journal = {Journal of Biological Chemistry},
title = {A human lectin array for characterizing host-pathogen interactions},
url = {http://dx.doi.org/10.1016/j.jbc.2024.107869},
volume = {300},
year = {2024}
}
RIS format (EndNote, RefMan)
TY - JOUR
AB - A human lectin array has been developed to probe the interactions of innate immune receptors with pathogenic and commensal micro-organisms. Following the successful introduction of a lectin array containing all of the cow C-type carbohydrate-recognition domains (CRDs), a human array described here contains the C-type CRDs as well as CRDs from other classes of sugar-binding receptors, including galectins, siglecs, R-type CRDs, ficolins, intelectins and chitinase-like lectins. The array is constructed with CRDs modified with single-site biotin tags, ensuring that the sugar-binding sites in CRDs are displayed on a streptavidin-coated surface in a defined orientation and are accessible to the surfaces of microbes. A common approach used for expression and display of CRDs from all of the different structural categories of glycan-binding receptors allows comparisons across lectin families. In addition to previously documented protocols for binding of fluorescently-labeled bacteria, methods have been developed for detecting unlabeled bacteria bound to the array by counter-staining with DNA binding dye. Screening has also been undertaken with viral glycoproteins and bacterial and fungal polysaccharides. The array provides an unbiased screen for sugar ligands that interact with receptors and many show binding not anticipated from earlier studies. For example, some of the galectins bind with high affinity to bacterial glycans that lack lactose or N acetyllactosamine. The results demonstrate the utility of the human lectin array for providing a unique overview of the interactions of multiple classes of glycan-binding proteins in the innate immune system with different types of micro-organisms.
AU - Benjamin,S
AU - Jégouzo,S
AU - Lieng,C
AU - Daniels,C
AU - Coispeau,M
AU - Lau,R
AU - Kim,S
AU - Metaxa,Y
AU - Philpott,J
AU - Li,T
AU - Dai,C
AU - Wang,X
AU - Newby,M
AU - Pier,G
AU - Crispin,M
AU - Clements,A
AU - Taylor,M
AU - Drickamer,K
DO - 10.1016/j.jbc.2024.107869
PY - 2024///
SN - 0021-9258
TI - A human lectin array for characterizing host-pathogen interactions
T2 - Journal of Biological Chemistry
UR - http://dx.doi.org/10.1016/j.jbc.2024.107869
UR - https://www.sciencedirect.com/science/article/pii/S0021925824023718?via%3Dihub
UR - http://hdl.handle.net/10044/1/115027
VL - 300
ER -