Iron acquisition and regulation systems in Streptococcus species

被引:41
作者
Ge, Ruiguang [1 ,2 ]
Sun, Xuesong [3 ]
机构
[1] Sun Yat Sen Univ, Coll Life Sci, Minist Educ, Key Lab Gene Engn, Guangzhou 510275, Guangdong, Peoples R China
[2] Sun Yat Sen Univ, Coll Life Sci, State Key Lab Biocontrol, Guangzhou 510275, Guangdong, Peoples R China
[3] Jinan Univ, Coll Life Sci & Technol, Inst Life & Hlth Engn, Key Lab Funct Prot Res,Guangdong Higher Educ Inst, Guangzhou 510632, Guangdong, Peoples R China
基金
中国国家自然科学基金;
关键词
CELL-SURFACE PROTEIN; HISTIDINE-RICH PROTEIN; SOLUTE-BINDING-PROTEIN; GROUP-A STREPTOCOCCUS; CRYSTAL-STRUCTURE; OXIDATIVE STRESS; ABC TRANSPORTER; HEME TRANSFER; PEROXIDE RESISTANCE; ENVIRONMENTAL HEME;
D O I
10.1039/c4mt00011k
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Gram-positive Streptococcus species are responsible for millions of cases of meningitis, bacterial pneumonia, endocarditis, erysipelas and necrotizing fasciitis. Iron is essential for the growth and survival of Streptococcus in the host environment. Streptococcus species have developed various mechanisms to uptake iron from an environment with limited available iron. Streptococcus can directly extract iron from host iron-containing proteins such as ferritin, transferrin, lactoferrin and hemoproteins, or indirectly by relying on the employment of specialized secreted hemophores (heme chelators) and small siderophore molecules (high affinity ferric chelators). This review presents the most recent discoveries in the iron acquisition system of Streptococcus species - the transporters as well as the regulators.
引用
收藏
页码:996 / 1003
页数:8
相关论文
共 91 条
[1]  
Aisen P, 1974, Adv Exp Med Biol, V48, P125
[2]   Bacterial iron homeostasis [J].
Andrews, SC ;
Robinson, AK ;
Rodríguez-Quiñones, F .
FEMS MICROBIOLOGY REVIEWS, 2003, 27 (2-3) :215-237
[3]  
Andrews S, 2013, METAL IONS LIFE SCI, V12, P203, DOI 10.1007/978-94-007-5561-1_7
[4]   Bis-methionyl coordination in the crystal structure of the heme-binding domain of the streptococcal cell surface protein shp [J].
Aranda, Roman ;
Worley, Chad E. ;
Liu, Mengyao ;
Bitto, Eduard ;
Cates, M. Susan ;
Olson, John S. ;
Lei, Benfang ;
Phillips, George N., Jr. .
JOURNAL OF MOLECULAR BIOLOGY, 2007, 374 (02) :374-383
[5]   Identification and characterization of a Streptococcus pyogenes operon involved in binding of hemoproteins and acquisition of iron [J].
Bates, CS ;
Montañez, GE ;
Woods, CR ;
Vincent, RM ;
Eichenbaum, Z .
INFECTION AND IMMUNITY, 2003, 71 (03) :1042-1055
[6]   Characterization of MtsR, a new metal regulator in group A streptococcus, involved in iron acquisition and virulence [J].
Bates, CS ;
Toukoki, C ;
Neely, MN ;
Eichenbaum, Z .
INFECTION AND IMMUNITY, 2005, 73 (09) :5743-5753
[7]   Molecular genetic anatomy of inter- and intraserotype variation in the human bacterial pathogen group A Streptococcus [J].
Beres, SB ;
Richter, EW ;
Nagiec, MJ ;
Sumby, P ;
Porcella, SF ;
Deleo, FR ;
Musser, JM .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2006, 103 (18) :7059-7064
[8]   Chemical aspects of siderophore mediated iron transport [J].
Boukhalfa, H ;
Crumbliss, AL .
BIOMETALS, 2002, 15 (04) :325-339
[9]   Expression of the MtsA lipoprotein of Streptococcus agalactiae A909 is regulated by manganese and iron [J].
Bray, Beverley A. ;
Sutcliffe, Iain C. ;
Harrington, Dean J. .
ANTONIE VAN LEEUWENHOEK INTERNATIONAL JOURNAL OF GENERAL AND MOLECULAR MICROBIOLOGY, 2009, 95 (01) :101-109
[10]   The PerR regulon in peroxide resistance and virulence of Streptococcus pyogenes [J].
Brenot, A ;
King, KY ;
Caparon, MG .
MOLECULAR MICROBIOLOGY, 2005, 55 (01) :221-234