Endolysins: redefining antibacterial therapy.

Bjorn Lars Herpers speaks to Natasha Leeson, Commissioning Editor: Bjorn Lars Herpers was born on 16 February 1974 in Schaesberg. In 1992 he graduated summa cum laude at Gymnasium Rolduc in Kerkrade (The Netherlands) and started to study medical biology at the University of Utrecht. After 3 years, he started to study medicine as well. He graduated cum laude in medical biology in 1999 and obtained his medical degree in 2001. After 1 year of residency in internal medicine at Gooi-Noord Hospital under supervision of DW Erkelens and P Niermeier, he switched to a residency in medical microbiology at the University Medical Center Utrecht and the St Antonius Hospital Nieuwegein under supervision of J Verhoef and B M de Jongh. During his residency, he started to work on his thesis on genetic polymorphisms in MBL and L-ficolin, two complement-activating pattern recognition receptors. In 2009 he became a medical microbiologist and joined the staff at the Regional Public Health Laboratory Kennemerland in Haarlem. Since 2012, he has been involved in clinical research on endolysin therapy in collaboration with Micreos in Bilthoven.

Coding and non-coding polymorphisms in the lectin pathway activator L-ficolin gene in 188 Dutch blood bank donors.

Human L-ficolin (FCN) is a serum lectin characterized by a collagen-like and a fibrinogen-like domain that can activate the lectin pathway of complement. Structural and functional similarities to mannose-binding lectin (MBL) suggest a role for L-ficolin in innate immunity. Structural polymorphisms in the MBL2 gene lead to functional deficiency of MBL. Polymorphisms in the FCN2 gene have not been studied previously. We developed 10 denaturing gradient gel electrophoresis (DGGE) assays to screen a total of 188 Dutch Caucasians for polymorphisms in FCN2. Total gene screening in this large cohort revealed 10 single nucleotide polymorphisms (SNPs). Interestingly, two conserved coding SNPs were found in exon 8, leading to amino acid substitutions within the fibrinogen-like domain. Fibrinogen-like domains are highly conserved among several proteins in many species. As this domain is responsible for binding of L-ficolin, these newly found coding polymorphisms could alter the affinity of the protein for its substrates and possibly alter the ability of L-ficolin to recognize invading microorganisms.