ArticleJournal of immunological methods2010
New monoclonal anti-mouse DC-SIGN antibodies reactive with acetone-fixed cells.
Article in Journal of immunological methods, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 15 citations in OpenAlex.
- Dendritic Cells and T Cells, Partners in Atherogenesis and the Translating Road Ahead.Frontiers in immunology · 2020Review
- Mouse DC-SIGN/CD209a as Target for Antigen Delivery and Adaptive Immunity.Frontiers in immunology · 2018Article
- Biochemical and immunological characterization of a novel monoclonal antibody against mouse leukotriene B4 receptor 1.PloS one · 2017Article
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- Vaccine strategies utilizing C-type lectin receptors on dendritic cells in vivo.Clinical and experimental vaccine research · 2014Review
- The role of the vascular dendritic cell network in atherosclerosis.American journal of physiology. Cell physiology · 2013Review
- In vivo T cell activation induces the formation of CD209(+) PDL-2(+) dendritic cells.PloS one · 2013Article
- PE-Cy5.5 conjugates bind to the cells expressing mouse DEC205/CD205.Journal of immunological methods · 2012Article
- Generation of anti-human DEC205/CD205 monoclonal antibodies that recognize epitopes conserved in different mammals.Journal of immunological methods · 2012Article
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- Article
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Authors and funding
11 authors at 2 institutions in 1 country.
Funding
Abstract
Mouse DC-SIGN CD209a is a type II transmembrane protein, one of a family of C-type lectin genes syntenic and homologous to human DC-SIGN. Current anti-mouse DC-SIGN monoclonal antibodies (MAbs) are unable to react with DC-SIGN in acetone-fixed cells, limiting the chance to visualize DC-SIGN in tissue sections. We first produced rabbit polyclonal PAb-DSCYT14 against a 14-aa peptide in the cytosolic domain of mouse DC-SIGN, and it specifically detected DC-SIGN and not the related lectins, SIGN-R1 and SIGN-R3 expressed in transfected CHO cells. MAbs were generated by immunizing rats and DC-SIGN knockout mice with the extracellular region of mouse DC-SIGN. Five rat IgG2a or IgM MAbs, named BMD10, 11, 24, 25, and 30, were selected and each MAb specifically detected DC-SIGN by FACS and Western blots, although BMD25 was cross-reactive to SIGN-R1. Two mouse IgG2c MAbs MMD2 and MMD3 interestingly bound mouse DC-SIGN but at 10 fold higher levels than the rat MAbs. When the binding epitopes of the new BMD and two other commercial rat anti-DC-SIGN MAbs, 5H10 and LWC06, were examined by competition assays, the epitopes of BMD11, 24, and LWC06 were identical or closely overlapping while BMD10, 30, and 5H10 were shown to bind different epitopes. MMD2 and MMD3 epitopes were on a 3rd noncompeting region of mouse DC-SIGN. DC-SIGN expressed on the cell surface was sensitive to collagenase treatment, as monitored by polyclonal and MAb. These new reagents should be helpful to probe the biology of DC-SIGN in vivo.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.