title: Heat-shock protein ClpL/HSP100 increases penicillin tolerance in Streptococcus pneumoniae.
abstract: Penicillin resistance and tolerance has been an increasing threat to the treatment of pneumococcal pneumoniae. However, no penicillin tolerance-related genes have been claimed. Here we show that a major heat shock protein ClpL/HSP100 could modulate the expression of a cell wall synthesis enzyme PBP2x, and subsequently increase cell wall thickness and penicillin tolerance in Streptococus pneumoniae.
authors.affiliation: School of Pharmacy, Sungkyunkwan University, Suwon, Korea.
authors.forename: Thao Dang-Hien
authors.initials: TD
authors.lastname: Tran
authors.forename: Hyog-Young
authors.initials: HY
authors.lastname: Kwon
authors.forename: Eun-Hye
authors.initials: EH
authors.lastname: Kim
authors.forename: Ki-Woo
authors.initials: KW
authors.lastname: Kim
authors.forename: David E
authors.initials: DE
authors.lastname: Briles
authors.forename: Suhkneung
authors.initials: S
authors.lastname: Pyo
authors.forename: Dong-Kwon
authors.initials: DK
authors.lastname: Rhee
mesh_terms: D001426:Bacterial Proteins / Q000187:drug effects / Q000378:metabolism*; D006360:Heat-Shock Proteins / Q000378:metabolism*; D006801:Humans; D010403:Penicillin Resistance; D046915:Penicillin-Binding Proteins / Q000378:metabolism*; D010406:Penicillins / Q000494:pharmacology*; D011008:Pneumococcal Infections / Q000188:drug therapy* / Q000378:metabolism / Q000382:microbiology; D013296:Streptococcus pneumoniae / Q000187:drug effects*
chemical_list: D001426:Bacterial Proteins; D006360:Heat-Shock Proteins; D046915:Penicillin-Binding Proteins; D010406:Penicillins; C072223:PBP 2x protein, Streptococcus