The β-Prism Lectin Domain ofVibrio choleraeHemolysin Promotes Self-assembly of the β-Pore-forming Toxin by a Carbohydrate-independent Mechanism

Functional Mapping of the Lectin Activity Site on the β-Prism Domain ofVibrio choleraeCytolysin

(2012) Anand Kumar Rai et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Vibrio cholerae Cytolysin Recognizes the Heptasaccharide Core of Complex N-Glycans with Nanomolar Affinity

(2012) Sophia Levan et al.   JOURNAL OF MOLECULAR BIOLOGY

Hemolysin Induces Toll-like Receptor (TLR)-independent Apoptosis and Multiple TLR-associated Parallel Activation of Macrophages

(2011) Deep Chandan Chakraborty et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Crystal structure of the Vibrio cholerae cytolysin heptamer reveals common features among disparate pore-forming toxins

(2011) S. De et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Role of a disintegrin and metalloprotease 10 in Staphylococcus aureus  -hemolysin-mediated cellular injury

(2010) G. A. Wilke et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Pore formation by Vibrio cholerae cytolysin follows the same archetypical mode as β-barrel toxins from gram-positive organisms

(2009) Sabine Löhner et al.   FASEB JOURNAL

Three-Dimensional Structure of Different Functional Forms of the Vibrio cholerae Hemolysin Oligomer: a Cryo-Electron Microscopic Study

(2009) S. Dutta et al.   JOURNAL OF BACTERIOLOGY

Vibrio cholerae cytolysin is essential for high enterotoxicity and apoptosis induction produced by a cholera toxin gene-negative V. cholerae non-O1, non-O139 strain

(2007) Hector Alex Saka et al.   MICROBIAL PATHOGENESIS

Vibrio cholerae hemolysin is apoptogenic to peritoneal B-1a cells but its oligomer shepherd the cells for IgA response

(2007) Gayatri Mukherjee et al.   MOLECULAR IMMUNOLOGY