Ho, M.R., Lou, Y.C., Wei, S.Y., Luo, S.C., Lin, W.C., Lyu, P.C. and Chen, C. (2010) Human Reg IV Protein Adopts a Typical C-Type Lectin Fold but Binds Mannan with Two Calcium-Independent Sites. Journal of Molecular Biology, 402, 682-695. https://doi.org/10.1016/j.jmb.2010.07.061

has been cited by the following article:

• TITLE: Recombinant Human REG Iα Aggregates Staphylococcus aureus—Exhibits a Lectin-Like Function

  AUTHORS: Nausheen Jamal, Yuichiro Kezuka, Takamasa Nonaka, Kazuaki Ohashi, Koji Nata

  KEYWORDS: Reg Proteins, Lectin-Like Activity, Bacterial Aggregation

  JOURNAL NAME: Advances in Bioscience and Biotechnology, Vol.8 No.3, March 16, 2017

  ABSTRACT: Staphylococcus aureus is pathogenic to humans with worldwide health care concern due to its ability to evade the immune system and develop resistance to multiple drugs. Reg family proteins are C-type lectins with antimicrobial properties. Bacterial aggregation through binding to microbial cell surface sugar and/or lipid moieties is key mechanism employed in the process. In the present study we have analysed the antimicrobial effect of human REG Iα on S. aureus. Aggregation of mid-log phase culture of S. aureus was observed in presence of purified recombinant REG Iα. Therefore REG Iα can be applied in eliminating S. aureus infections in humans.