Diversity in bacterial lysis systems: bacteriophages show the way

被引:177
作者
Catalao, Maria Joao [1 ]
Gil, Filipa [1 ]
Moniz-Pereira, Jose [1 ]
Sao-Jose, Carlos [1 ]
Pimentel, Madalena [1 ]
机构
[1] Univ Lisbon, Fac Pharm, Unidade Retrovirus & Infeccoes Associadas, Ctr Patogenese Mol, P-1649003 Lisbon, Portugal
关键词
endolysins; holins; LysB; phage lysis; secreted endolysins; spanins; MYCOBACTERIOPHAGE MS6 ENCODES; N-TERMINAL REGION; OUTER-MEMBRANE; LAMBDA-S; BACILLUS-SUBTILIS; TRANSCRIPTION TERMINATION; FUNCTIONAL-ANALYSIS; PHAGE; HOLIN; GENE;
D O I
10.1111/1574-6976.12006
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Bacteriophages have developed multiple host cell lysis strategies to promote release of descendant virions from infected bacteria. This review is focused on the lysis mechanisms employed by tailed double-stranded DNA bacteriophages, where new developments have recently emerged. These phages seem to use a least common denominator to induce lysis, the so-called holin-endolysin dyad. Endolysins are cell wall-degrading enzymes whereas holins form holes' in the cytoplasmic membrane at a precise scheduled time. The latter function was long viewed as essential to provide a pathway for endolysin escape to the cell wall. However, recent studies have shown that phages can also exploit the host cell secretion machinery to deliver endolysins to their target and subvert the bacterial autolytic arsenal to effectively accomplish lysis. In these systems the membrane-depolarizing holin function still seems to be essential to activate secreted endolysins. New lysis players have also been uncovered that promote degradation of particular bacterial cell envelopes, such as that of mycobacteria.
引用
收藏
页码:554 / 571
页数:18
相关论文
共 115 条
[1]  
Ackermann Hans-W., 2009, V501, P127, DOI 10.1007/978-1-60327-164-6_13
[2]   The complete nucleotide sequence and functional organization of Bacillus subtilis bacteriophage SPP1 [J].
Alonso, JC ;
Lüder, G ;
Stiege, AC ;
Chai, SH ;
Weise, F ;
Trautner, TA .
GENE, 1997, 204 (1-2) :201-212
[3]   Transcript map of the temperate Lactobacillus gasseri bacteriophage φadh [J].
Altermann, E ;
Henrich, B .
MICROBIOLOGY-SGM, 2003, 149 :2987-2999
[4]   Characterization of the dual start motif of a class II holin gene [J].
Barenboim, M ;
Chang, CY ;
Hajj, FD ;
Young, R .
MOLECULAR MICROBIOLOGY, 1999, 32 (04) :715-727
[5]   Breaking free: "Protein antibiotics" and phage lysis [J].
Bernhardt, TG ;
Wang, IN ;
Struck, DK ;
Young, R .
RESEARCH IN MICROBIOLOGY, 2002, 153 (08) :493-501
[6]   The lysis protein E of φX174 is a specific inhibitor of the MraY-catalyzed step in peptidoglycan synthesis [J].
Bernhardt, TG ;
Struck, DK ;
Young, R .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2001, 276 (09) :6093-6097
[7]   A protein antibiotic in the phage Qβ virion:: Diversity in lysis targets [J].
Bernhardt, TG ;
Wang, IN ;
Struck, DK ;
Young, R .
SCIENCE, 2001, 292 (5525) :2326-2329
[8]   The final step in the phage infection cycle: the Rz and Rz1 lysis proteins link the inner and outer membranes [J].
Berry, Joel ;
Summer, Elizabeth J. ;
Struck, Douglas K. ;
Young, Ryland .
MOLECULAR MICROBIOLOGY, 2008, 70 (02) :341-351
[9]   The lambda spanin components Rz and Rz1 undergo tertiary and quaternary rearrangements upon complex formation [J].
Berry, Joel ;
Savva, Christos ;
Holzenburg, Andreas ;
Young, Ry .
PROTEIN SCIENCE, 2010, 19 (10) :1967-1977
[10]   Teichoic acid is an essential polymer in Bacillus subtilis that is functionally distinct from teichuronic acid [J].
Bhavsar, AP ;
Erdman, LK ;
Schertzer, JW ;
Brown, ED .
JOURNAL OF BACTERIOLOGY, 2004, 186 (23) :7865-7873