E
Erwin De Genst
Researcher at Vrije Universiteit Brussel
Publications - 15
Citations - 2442
Erwin De Genst is an academic researcher from Vrije Universiteit Brussel. The author has contributed to research in topics: Single-domain antibody & Bacterial adhesin. The author has an hindex of 14, co-authored 15 publications receiving 2248 citations. Previous affiliations of Erwin De Genst include Flanders Institute for Biotechnology.
Papers
More filters
Journal ArticleDOI
Molecular basis for the preferential cleft recognition by dromedary heavy-chain antibodies.
Erwin De Genst,Karen Silence,Klaas Decanniere,Katja Conrath,Remy Loris,Jörg Kinne,Serge Muyldermans,Lode Wyns +7 more
TL;DR: A single domain antigen-combining site has a clear structural advantage over a conventional dimeric format for targeting clefts on antigenic surfaces with a pronounced preference for heavy-chain antibodies of camelids.
Journal ArticleDOI
Potent enzyme inhibitors derived from dromedary heavy‐chain antibodies
Marc Lauwereys,Mehdi Arbabi Ghahroudi,Aline Desmyter,Jörg Kinne,Wolfgang Hölzer,Erwin De Genst,Lode Wyns,Serge Muyldermans +7 more
TL;DR: Evidence is provided that dromedary heavy‐chain antibodies, in vivo‐matured in the absence of light chains, are a unique source of inhibitory antibodies that appear to be potent enzyme inhibitors when tested in chromogenic assays.
Journal ArticleDOI
Receptor binding studies disclose a novel class of high-affinity inhibitors of the Escherichia coli FimH adhesin
Julie Bouckaert,Jenny Berglund,Mark A. Schembri,Erwin De Genst,Lieve Cools,Manfred Wuhrer,Chia-Suei Hung,Jerome S. Pinkner,Rikard Slättegård,Anton V. Zavialov,Devapriya Choudhury,Solomon Langermann,Scott J. Hultgren,Lode Wyns,Per Klemm,Stefan Oscarson,Stefan D. Knight,Henri De Greve +17 more
TL;DR: These relative FimH affinities correlate exceptionally well with the relative concentrations of the same glycans needed for the inhibition of adherence of type 1 piliated E. coli.
Journal ArticleDOI
Antibody repertoire development in camelids.
TL;DR: Interestingly, antigen-specific VHHs are easily retrieved after panning of a phage-displayed rearranged V-gene pool cloned from an immunised camelid, and possess a number of biophysical properties that offer particular advantages in various medical and biotechnological applications.
Journal ArticleDOI
Molecular basis of gyrase poisoning by the addiction toxin CcdB.
M.-H. Dao-Thi,Laurence Van Melderen,Erwin De Genst,Hassan Afif,Lieven Buts,Lode Wyns,Remy Loris +6 more
TL;DR: Overexpression of GyrA14 protects Escherichia coli cells against CCDB, mimicking the action of the antidote CcdA, and explains why the Arg462Cys mutation in the A subunit of gyrase confers resistance to CcdB.