Collagen VI encodes antimicrobial activity: Novel innate host defense properties of the extracellular matrix

Journal of Innate Immunity

Volumn 4, Issue 4, 2012, Pages 371-376

  Abdillahi, Suado M ^a   Balvanovic, Selma ^a   Baumgarten, Maria ^a   Mörgelin, Matthias ^a  

^a LUND UNIVERSITY   (Sweden)

Author keywords

Antimicrobial activity; Collagen type VI; Extracellular matrix; Innate host defense; Oral pathogens; Streptococcus

Indexed keywords

CATHELICIDIN ANTIMICROBIAL PEPTIDE LL 37; COLLAGEN TYPE 6;

ANIMAL TISSUE; ANTIMICROBIAL ACTIVITY; ARTICLE; CONTROLLED STUDY; EXTRACELLULAR MATRIX; INNATE IMMUNITY; NONHUMAN; PRIORITY JOURNAL; STREPTOCOCCUS GROUP A; STREPTOCOCCUS GROUP C; STREPTOCOCCUS GROUP G;

ANTI-INFECTIVE AGENTS; COLLAGEN TYPE VI; EXTRACELLULAR MATRIX; HUMANS; IMMUNITY, INNATE; MICROBIAL SENSITIVITY TESTS; STREPTOCOCCUS; STREPTOCOCCUS PYOGENES;

EID: 84863335308     PISSN: 1662811X     EISSN: 16628128     Source Type: Journal    
DOI: 10.1159/000335239     Document Type: Article

References (26)

1. Bober M, Enochsson C, Collin M, Mörgelin M: Collagen VI is a subepithelial adhesive target for human respiratory tract pathogens. J Innate Immun 2010; 2: 160-166.
2. Gara SK, Grumati P, Squarzoni S, Sabatelli P, Urciuolo A, Bonaldo P, Paulsson M, Wagener R: Differential and restricted expression of novel collagen VI chains in mouse. Matrix Biol 2011; 30: 248-257.
3. Tooley LD, Zamurs LK, Beecher N, Baker NL, Peat RA, Adams NE, Bateman JF, North KN, Baldock C, Lamande SR: Collagen VI microfibril formation is abolished by an {alpha}2(VI) von Willebrand factor type A domain mutation in a patient with Ullrich congenital muscular dystrophy. J Biol Chem 2010; 285: 33567-33576.
4. Fitzgerald J, Rich C, Zhou FH, Hansen U: Three novel collagen VI chains, alpha4(VI), alpha5(VI), and alpha6(VI). J Biol Chem 2008; 283: 20170-20180.
5. Specks U, Mayer U, Nischt R, Spissinger T, Mann K, Timpl R, Engel J, Chu ML: Structure of recombinant N-terminal globule of type VI collagen alpha 3 chain and its binding to heparin and hyaluronan. EMBO J 1992; 11: 4281-4290.
6. Andersson E, Rydeng'rd V, Sonesson A, Mörgelin M, Björck, L, Schmidtchen A: Antimicrobial activities of heparin-binding peptides. Eur J Biochem 2004; 271: 1219-1226.
7. Oehmcke S, Shannon O, Mörgelin M, Herwald H: Streptococcal M proteins and their role as virulence determinants. Clin Chim Acta 2010; 411: 1172-1180.
8. Oster HR, Bisno AL: Group C and Group G streptococcal infections: epidemiologic and clinical aspects; in Fischetti VA, Novik RP, Ferretti JJ, Portnoy DA, Rood JIeds): The Gram-Positive Pathogens. Washington, American Society for Microbiology, 2000, pp 184-190.
9. Haidan A, Talay SR, Rohde M, Sriprakash KS, Currie BJ, Chhatwal GS: Pharyngeal carriage of group C and group G streptococci and acute rheumatic fever in an Aboriginal population. Lancet 2000; 356: 1167-1169.
10. Dinkla K, Rohde M, Jansen WT, Carapetis JR, Chhatwal GS, Talay SR: Streptococcus pyogenes recruits collagen via surface-bound fibronectin: a novel colonization and immune evasion mechanism. Mol Microbiol 2003; 47: 861-869.
11. Patti JM, Allen BL, McGavin MJ, Höök M: MSCRAMM-mediated adherence of microorganisms to host tissues. Annu Rev Microbiol 1994; 48: 585-617.
12. Nitsche DP, Johansson HM, Frick IM, Mörgelin M: Streptococcal protein FOG, a novel matrix adhesin interacting with collagen I in vivo. J Biol Chem 2006; 281: 1670-1679.
13. Hallström T, Singh B, Resman F, M Blom A, Mörgelin M, Riesbeck K: Haemophilus influenzae protein E binds to the extracellular matrix by concurrently interacting with laminin and vitronectin. J Infect Dis 2011; 204: 1065-1074.
14. Kihlberg BM, Collin M, Olsen A, Björck L: Protein H, an antiphagocytic surface protein in Streptococcus pyogenes. Infect Immun 1999; 67: 1708-1714.
15. Mjörner H, Albertsson P', Kronwall G: Isoelectric points and surface hydrophobicity of gram-positive cocci as determined by crosspartition and hydrophobic affinity partition in aqueous two-phase systems. Infect Immun 1982; 36: 227-234.
16. Kronwall G, Myhre EB, Björck L, Bergg'rd I: Binding of aggregated human 2-microglobulin to surface protein structure in group A, C and G streptococci. Infect Immun 1978; 22: 136-142.
17. Widebäck K, Seal US, Kronwall G: Receptor in group C and G streptococci detects albumin structures present in mammalian species. Infect Immun 1982; 36: 469-475.
18. Spissinger T, Engel J: Type VI collagen beaded microfibrils from bovine cornea depolymerize at acidic pH, and depolymerization and polymerization are not influenced by hyaluronan. Matrix Biol 1995; 14: 499-505.
19. Oehmcke S, Mörgelin M, Herwald H: Activation of the human contact system on neutrophil extracellular traps. J Innate Immun 2009; 1: 225-230.
20. Sörensen OE, Follin P, Johnsen AH, Calafat J, Tjabranga GS, Hiemstra PS, Borregaard N: Human cathelicidin, hCAP-18, is processed to the antimicrobial peptide LL-37 by extracellular cleavage with proteinase 3. Blood 2001; 97: 3951-3959.
21. Brennan EP, Reing J, Chew D, Myers-Irvin JM, Young EJ, Badylak SF: Antibacterial activity within degradation products of biological scaffolds composed of extracellular matrix. Tissue Eng 2006; 12: 2949-2955.
22. Senÿrek I, Klein G, Kalbacher H, Deeg M, Schittek B: Peptides derived from the human laminin a4 and a5 chains exhibit antimicrobial activity. Peptides 2010; 31: 1468-1472.
23. Malmsten M, Davoudi M, Schmidtchen A: Bacterial killing by heparin-binding peptides from PRELP and thrombospondin. Matrix Biol 2006; 25: 294-300.
24. Malmsten M, Davoudi M, Walse B, Rydeng'rd V, Pasupuleti M, Mörgelin M, Schmidtchen A: Antimicrobial peptides derived from growth factors. Growth Factors 2007; 25: 60-70.
25. Malmström E, Mörgelin M, Malmsten M, Johansson L, Norrby-Teglund A, Shannon O, Schmidtchen A, Meijers JC, Herwald H: Protein C inhibitor - a novel antimicrobial agent. PLoS Pathog 2009; 5:e1000698.
26. Kasetty G, Papareddy P, Kalle M, Rydeng'rd V, Mörgelin M, Albiger B, Malmsten M, Schmidtchen A: The C-terminal sequence of several human serine proteases encodes host defense functions. J Innate Immun 2011; 3: 471-482.