Sequence-structure relationships in polysaccharide co-polymerase (PCP) proteins.

Polysaccharides are ubiquitously distributed on the cell surface of bacteria. These polymers are involved in many processes, including immune avoidance and bacteria-host interactions, which are especially important for pathogenic organisms. In many instances, the lengths of these polysaccharides are not random, but rather distribute around some mean value, termed the modal length. A large family of proteins, called polysaccharide co-polymerases (PCPs), found in both Gram-negative and Gram-positive species regulate polysaccharide modal length. Recent crystal structures of Wzz proteins from Escherichia coli and Salmonella typhimurium provide the first atomic-resolution information for one family of PCPs, the PCP1 group. These crystal structures have important implications for the structures of other PCP families.

[1]  Julian Parkhill,et al.  Genetic Analysis of the Capsular Biosynthetic Locus from All 90 Pneumococcal Serotypes , 2006, PLoS genetics.

[2]  R. Morona,et al.  Molecular, genetic, and topological characterization of O-antigen chain length regulation in Shigella flexneri , 1995, Journal of bacteriology.

[3]  P. Alifano,et al.  Nucleotide sequences of the genes regulating O-polysaccharide antigen chain length (rol) from Escherichia coli and Salmonella typhimurium: protein homology and functional complementation , 1992, Journal of bacteriology.

[4]  P. Reeves,et al.  Repeat unit polysaccharides of bacteria: a model for polymerization resembling that of ribosomes and fatty acid synthetase, with a novel mechanism for determining chain length , 1993, Molecular microbiology.

[5]  C. Whitfield,et al.  Impact of Phosphorylation of Specific Residues in the Tyrosine Autokinase, Wzc, on Its Activity in Assembly of Group 1 Capsules in Escherichia coli , 2002, Journal of bacteriology.

[6]  C. Whitfield,et al.  Functional Analysis of Conserved Gene Products Involved in Assembly of Escherichia coli Capsules and Exopolysaccharides: Evidence for Molecular Recognition between Wza and Wzc for Colanic Acid Biosynthesis , 2005, Journal of bacteriology.

[7]  C. Geourjon,et al.  Staphylococcus aureus Operates Protein-tyrosine Phosphorylation through a Specific Mechanism* , 2006, Journal of Biological Chemistry.

[8]  Ivan Mijakovic,et al.  Tyrosine phosphorylation: an emerging regulatory device of bacterial physiology. , 2007, Trends in biochemical sciences.

[9]  R. Morona,et al.  Evaluation of Wzz/MPA1/MPA2 proteins based on the presence of coiled-coil regions. , 2000, Microbiology.

[10]  Ivan Mijakovic,et al.  Structural Basis for the Regulation Mechanism of the Tyrosine Kinase CapB from Staphylococcus aureus , 2008, PLoS biology.

[11]  L. Burrows,et al.  Pseudomonas aeruginosa B-band O-antigen chain length is modulated by Wzz (Ro1) , 1997, Journal of bacteriology.

[12]  Zongchao Jia,et al.  Structure of Escherichia coli tyrosine kinase Etk reveals a novel activation mechanism , 2008, The EMBO journal.

[13]  P. Reeves,et al.  A plasmid-borne O-antigen chain length determinant and its relationship to other chain length determinants. , 1995, FEMS microbiology letters.

[14]  J. Rubinstein,et al.  Bacterial polysaccharide co-polymerases share a common framework for control of polymer length , 2008, Nature Structural &Molecular Biology.

[15]  S. Payne,et al.  Effect of mutations in Shigella flexneri chromosomal and plasmid‐encoded lipopolysaccharide genes on invasion and serum resistance , 1997, Molecular microbiology.

[16]  R. Morona,et al.  Analysis of Shigella flexneri Wzz (Rol) function by mutagenesis and cross‐linking: Wzz is able to oligomerize , 1999, Molecular microbiology.

[17]  James H. Naismith,et al.  Wza the translocon for E. coli capsular polysaccharides defines a new class of membrane protein , 2006, Nature.

[18]  M. Tsai,et al.  Investigation of the conformational states of Wzz and the Wzz.O-antigen complex under near-physiological conditions. , 2007, Biochemistry.

[19]  R. Morona,et al.  Comparative Genetics of Capsular Polysaccharide Biosynthesis in Streptococcus pneumoniae Types Belonging to Serogroup 19 , 1999, Journal of bacteriology.

[20]  C. Whitfield,et al.  Phosphorylation of Wzc, a Tyrosine Autokinase, Is Essential for Assembly of Group 1 Capsular Polysaccharides in Escherichia coli* , 2001, The Journal of Biological Chemistry.

[21]  C. Whitfield,et al.  Lipopolysaccharide endotoxins. , 2002, Annual review of biochemistry.

[22]  J. Klena,et al.  The Modality of Enterobacterial Common Antigen Polysaccharide Chain Lengths Is Regulated by o349 of thewec Gene Cluster of Escherichia coliK-12 , 1999, Journal of bacteriology.

[23]  S. Attridge,et al.  Inducible serum resistance in Salmonella typhimurium is dependent on wzz(fepE)-regulated very long O antigen chains. , 2005, Microbes and infection.

[24]  C. Whitfield Biosynthesis and assembly of capsular polysaccharides in Escherichia coli. , 2006, Annual review of biochemistry.

[25]  M. Valvano,et al.  Functional Analysis of Predicted Coiled-Coil Regions in the Escherichia coli K-12 O-Antigen Polysaccharide Chain Length Determinant Wzz , 2008, Journal of bacteriology.

[26]  R. Morona,et al.  Analysis of the 5′ Portion of the Type 19A Capsule Locus Identifies Two Classes of cpsC, cpsD, andcpsE Genes in Streptococcus pneumoniae , 1999, Journal of bacteriology.

[27]  Hongjie Guo,et al.  Overexpression and characterization of Wzz of Escherichia coli O86:H2. , 2006, Protein expression and purification.

[28]  K. Timmis,et al.  Influence of different rol gene products on the chain length of Shigella dysenteriae type 1 lipopolysaccharide O antigen expressed by Shigella flexneri carrier strains , 1997, Journal of bacteriology.

[29]  G. Walker,et al.  Genes needed for the modification, polymerization, export, and processing of succinoglycan by Rhizobium meliloti: a model for succinoglycan biosynthesis , 1993, Journal of bacteriology.

[30]  A. Becker,et al.  The Molecular Weight Distribution of Succinoglycan Produced by Sinorhizobium meliloti Is Influenced by Specific Tyrosine Phosphorylation and ATPase Activity of the Cytoplasmic Domain of the ExoP Protein , 2001, Journal of bacteriology.

[31]  R. Morona,et al.  Coiled-coil regions play a role in the function of the Shigella flexneri O-antigen chain length regulator WzzpHS2. , 2008, Microbiology.

[32]  I. Roberts,et al.  The cell surface expression of group 2 capsular polysaccharides in Escherichia coli: the role of KpsD, RhsA and a multi‐protein complex at the pole of the cell , 2006, Molecular microbiology.

[33]  P. Reeves,et al.  The Wzz (Cld) Protein in Escherichia coli: Amino Acid Sequence Variation Determines O-Antigen Chain Length Specificity , 1998, Journal of bacteriology.

[34]  S. Attridge,et al.  Altering the Length of the Lipopolysaccharide O Antigen Has an Impact on the Interaction of Salmonella enterica Serovar Typhimurium with Macrophages and Complement , 2006, Journal of bacteriology.

[35]  G. Harauz,et al.  Translocation of Group 1 Capsular Polysaccharide in Escherichia coli Serotype K30 , 2003, Journal of Biological Chemistry.

[36]  J. Dubochet,et al.  Cryo-Transmission Electron Microscopy of Frozen-Hydrated Sections of Escherichia coli and Pseudomonas aeruginosa , 2003, Journal of bacteriology.

[37]  C. Whitfield,et al.  The 3D structure of a periplasm-spanning platform required for assembly of group 1 capsular polysaccharides in Escherichia coli , 2007, Proceedings of the National Academy of Sciences.

[38]  C. Whitfield,et al.  Periplasmic Protein-Protein Contacts in the Inner Membrane Protein Wzc Form a Tetrameric Complex Required for the Assembly of Escherichia coli Group 1 Capsules* , 2006, Journal of Biological Chemistry.

[39]  C. Arrecubieta,et al.  The Transport of Group 2 Capsular Polysaccharides across the Periplasmic Space in Escherichia coli , 2001, The Journal of Biological Chemistry.

[40]  M. Aebi,et al.  Interplay of the Wzx Translocase and the Corresponding Polymerase and Chain LengthRegulator Proteins in the Translocation and Periplasmic Assembly of Lipopolysaccharide O Antigen , 2006, Journal of bacteriology.

[41]  R. Morona,et al.  Regulation of O‐antigen chain length is required for Shigella flexneri virulence , 1997, Molecular microbiology.