Yet more intramolecular cross-links in Gram-positive surface proteins

Proceedings of the National Academy of Sciences of the United States of America

Volumn 111, Issue 4, 2014, Pages 1229-1230

  Schwarz Linek, Ulrich ^a   Banfield, Mark J ^b  

^a UNIVERSITY OF ST ANDREWS   (United Kingdom)

^b JOHN INNES CENTRE   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN;

CLOSTRIDIUM PERFRINGENS; CROSS LINKING; GRAM POSITIVE BACTERIUM; NONHUMAN; NOTE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN STRUCTURE; STREPTOCOCCUS PYOGENES;

ADHESINS, BACTERIAL; CLOSTRIDIUM PERFRINGENS; GLYCINE; IMMUNOGLOBULINS; THREONINE;

EID: 84893372980     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1322482111     Document Type: Note

References (20)

1. Kwon H, Squire CJ, Young PG, Baker EN (2014) Autocatalytically generated Thr-Gln ester bond cross-links stabilize the repetitive Igdomain shaft of a bacterial cell surface adhesin. Proc Natl Acad Sci USA 111:1367-1372.
2. Paterson GK, Mitchell TJ (2004) The biology of Gram-positive sortase enzymes. Trends Microbiol 12(2):89-95.
3. Proft T, Baker EN (2009) Pili in Gram-negative and Gram-positive bacteria-Structure, assembly and their role in disease. Cell Mol Life Sci 66(4):613-635.
4. Mora M, et al. (2005) Group A Streptococcus produce pilus-like structures containing protective antigens and Lancefield T antigens. Proc Natl Acad Sci USA 102(43):15641-15646.
5. Lauer P, et al. (2005) Genome analysis reveals pili in Group B Streptococcus. Science 309(5731):105.
6. Kang HJ, Coulibaly F, Clow F, Proft T, Baker EN (2007) Stabilizing isopeptide bonds revealed in gram-positive bacterial pilus structure. Science 318(5856):1625-1628.
7. Hendrickx AP, Budzik JM, Oh SY, Schneewind O (2011) Architects at the bacterial surface-Sortases and the assembly of pili with isopeptide bonds. Nat Rev Microbiol 9(3):166-176.
8. Kang HJ, Baker EN (2011) Intramolecular isopeptide bonds: Protein crosslinks built for stress? Trends Biochem Sci 36(4):229-237.
9. Kang HJ, Baker EN (2012) Structure and assembly of Gram-positive bacterial pili: Unique covalent polymers. Curr Opin Struct Biol 22(2): 200-207.
10. Hagan RM, et al. (2010) NMR spectroscopic and theoretical analysis of a spontaneously formed Lys-Asp isopeptide bond. Angew Chem Int Ed Engl 49(45):8421-8425.
11. Pointon JA, et al. (2010) A highly unusual thioester bond in a pilus adhesin is required for efficient host cell interaction. J Biol Chem 285(44):33858-33866.
12. Walden M, Crow A, Nelson MD, Banfield MJ (2013) Intramolecular isopeptide but not internal thioester bonds confer proteolytic and significant thermal stability to the S. pyogenes pilus adhesin Spy0125. Proteins, 10.1002/prot.24420.
13. Izoré T, et al. (2010) Structural basis of host cell recognition by the pilus adhesin from Streptococcus pneumoniae. Structure 18(1): 106-115.
14. Kang HJ, Baker EN (2009) Intramolecular isopeptide bonds give thermodynamic and proteolytic stability to the major pilin protein of Streptococcus pyogenes. J Biol Chem 284(31): 20729-20737.
15. El Mortaji L, Terrasse R, Dessen A, Vernet T, Di Guilmi AM (2010) Stability and assembly of pilus subunits of Streptococcus pneumoniae. J Biol Chem 285(16):12405-12415.
16. Alegre-Cebollada J, Badilla CL, Fernández JM (2010) Isopeptide bonds block the mechanical extension of pili in pathogenic Streptococcus pyogenes. J Biol Chem 285(15):11235-11242.
17. Hu X, et al. (2011) Autocatalytic intramolecular isopeptide bond formation in gram-positive bacterial pili: A QM/MM simulation. J Am Chem Soc 133(3):478-485.
18. Law SK, Dodds AW (1997) The internal thioester and the covalent binding properties of the complement proteins C3 and C4. Protein Sci 6(2):263-274.
19. Linke-Winnebeck C, et al. (2013) Structural model for the covalent adhesion of the Streptococcus pyogenes pilus through a thioester bond. J Biol Chem, 10.1074/jbc.M113.523761.
20. Allen WJ, Phan G, Waksman G (2012) Pilus biogenesis at the outer membrane of Gram-negative bacterial pathogens. Curr Opin Struct Biol 22(4):500-506.