Endolysins: redefining antibacterial therapy.

نویسندگان

  • Bjorn Lars Herpers
  • Natasha Leeson
چکیده

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.

برای دانلود رایگان متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Characterization of Modular Bacteriophage Endolysins from Myoviridae Phages OBP, 201ϕ2-1 and PVP-SE1

Peptidoglycan lytic enzymes (endolysins) induce bacterial host cell lysis in the late phase of the lytic bacteriophage replication cycle. Endolysins OBPgp279 (from Pseudomonas fluorescens phage OBP), PVP-SE1gp146 (Salmonella enterica serovar Enteritidis phage PVP-SE1) and 201φ2-1gp229 (Pseudomonas chlororaphis phage 201φ2-1) all possess a modular structure with an N-terminal cell wall binding d...

متن کامل

Synthesis of bacteriophage lytic proteins against Streptococcus pneumoniae in the chloroplast of Chlamydomonas reinhardtii

There is a pressing need to develop novel antibacterial agents given the widespread antibiotic resistance among pathogenic bacteria and the low specificity of the drugs available. Endolysins are antibacterial proteins that are produced by bacteriophage-infected cells to digest the bacterial cell wall for phage progeny release at the end of the lytic cycle. These highly efficient enzymes show a ...

متن کامل

‘Artilysation’ of endolysin λSa2lys strongly improves its enzymatic and antibacterial activity against streptococci

Endolysins constitute a promising class of antibacterials against Gram-positive bacteria. Recently, endolysins have been engineered with selected peptides to obtain a new generation of lytic proteins, Artilysins, with specific activity against Gram-negative bacteria. Here, we demonstrate that artilysation can also be used to enhance the antibacterial activity of endolysins against Gram-positive...

متن کامل

Adapting Drug Approval Pathways for Bacteriophage-Based Therapeutics

The global rise of multi-drug resistant bacteria has resulted in the notion that an "antibiotic apocalypse" is fast approaching. This has led to a number of well publicized calls for global funding initiatives to develop new antibacterial agents. The long clinical history of phage therapy in Eastern Europe, combined with more recent in vitro and in vivo success, demonstrates the potential for w...

متن کامل

Taking aim on bacterial pathogens: from phage therapy to enzybiotics.

The bactericidal activity of bacteriophages has been used to treat human infections for years as an alternative or a complement to antibiotic therapy. Nowadays, endolysins (phage-encoded enzymes that break down bacterial peptidoglycan at the terminal stage of the phage reproduction cycle) have been used successfully to control antibiotic-resistant pathogenic bacteria in animal models. Their cel...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

عنوان ژورنال:
  • Future microbiology

دوره 10 3  شماره 

صفحات  -

تاریخ انتشار 2015