| 1. |
- Hulting, Greta, et al.
(författare)
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Two novel IgG endopeptidases of Streptococcus equi
- 2009
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Ingår i: FEMS Microbiology Letters. - : Oxford University Press (OUP). - 1574-6968 .- 0378-1097. ; 298:1, s. 44-50
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Tidskriftsartikel (refereegranskat)abstract
- Streptococcus equi ssp. equi causes strangles, a highly contagious and serious disease in the upper respiratory tract of horses. Streptococcus equi ssp. zooepidemicus, another subspecies of this genus, is regarded as an opportunistic commensal in horses. The present study describes the characterization of two novel immunoglobulin G (IgG) endopeptidases of these subspecies, IdeE2 and IdeZ2. Both enzymes display sequence similarities with two previously characterized IgG endopeptidases, IdeE of S. equi ssp. equi and IdeZ of S. equi ssp. zooepidemicus. IdeE2 and IdeZ2 display high substrate-specificity in comparison with IdeE and IdeZ, as they both completely cleave horse IgG, while the activity against IgG from mouse, rabbit, cat, cow, sheep and goat is low or absent. The potential use of IdeE and IdeE2 as vaccine components was studied in a mouse infection model. In this vaccination and challenge study, both enzymes induced protection against S. equi ssp. equi infection.
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| 2. |
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| 3. |
- Bjerketorp, Joakim, et al.
(författare)
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A novel von Willebrand factor binding protein expressed by Staphylococcus aureus
- 2002
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Ingår i: Microbiology. - : Microbiology Society. - 1465-2080 .- 1350-0872. ; 148, s. 2037-2044
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Tidskriftsartikel (refereegranskat)abstract
- When a shotgun phage-display library of Staphylococcus aureus Newman was affinity selected (panned) against recombinant von Willebrand factor (vWf), a novel von Willebrand factor binding protein (vWbp) was found. Experimental data indicate that the interaction between vWbp and vWf is very specific and mediated by a region of 26 aa residues in the C-terminal part of vWbp. vWbp has an N-terminal secretory signal sequence but no cell wall anchoring motif, suggesting a soluble extracellular location. Mature vWbp could be purified from the culture supernatant and the identity of the protein was confirmed by N-terminal sequencing. vWbp migrates with an apparent molecular mass of 66 kDa and the deduced protein consists of 482 aa. The gene encoding vWbp, named vwb, was present in all S. aureus strains investigated.
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| 4. |
- Colque-Navarro, Patricia, et al.
(författare)
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Levels of antibody against 11 Staphylococcus aureus antigens in a healthy population.
- 2010
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Ingår i: Clinical and vaccine immunology : CVI. - 1556-679X. ; 17:7, s. 1117-23
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Tidskriftsartikel (refereegranskat)abstract
- Serum samples from 151 healthy individuals aged from 15 to 89 years were investigated by enzyme-linked immunosorbent assay (ELISA) for IgG levels against 11 different purified antigens from Staphylococcus aureus. Surface antigens, such as teichoic acid, clumping factors A and B, and bone sialoprotein binding protein, and extracellular proteins, such as alpha-toxin, lipase, enterotoxin A, toxic shock syndrome toxin, scalded-skin syndrome toxin, fibrinogen binding protein, and extracellular adherence protein, were used. The IgG values were analyzed in relation to the state of nasal carriage at the time of sampling. There was great individual variation in antibody levels in both young and elderly healthy subjects. Occurrence of S. aureus in the nares at the time of sampling was correlated with higher antibody levels, while elderly individuals over 65 years of age showed slightly lower levels than younger adults. More individuals than was expected from random probability calculations showed high antibody levels against several antigens, and more individuals than would be expected showed low levels against several antigens. Certain extracellular proteins had more often induced IgG levels of the same magnitude in the same individuals, indicating that among these individuals, there was a tendency to respond to certain antigens in the same way. Most individuals had circulating IgG antibodies to the 11 tested antigens, and some individuals had the tendency to be "good responders" to several antigens, while others were "poor responders." These findings constitute basic knowledge for the development of improved serological diagnostics, immune prophylaxis, individual prognosis tools, and therapy against invasive Staphylococcus aureus infections.
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| 5. |
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| 6. |
- Nelson, Annika, et al.
(författare)
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Staphylococcus epidermidis Isolated From Newborn Infants Express Pilus-Like Structures and Are Inhibited by the Cathelicidin-Derived Antimicrobial Peptide LL37
- 2009
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Ingår i: Pediatric Research. - 0031-3998 .- 1530-0447. ; 66:2, s. 174-178
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Tidskriftsartikel (refereegranskat)abstract
- Coagulase-negative staphylococci and its subtype Staphylococcus epidermidis are major indigenous Gram-positive inhabitants of the human skin. Colonization occurs in direct connection with birth and terrestrial adaptation. This study focuses on factors that may influence skin colonization of the newborn infant that relates to the immune status of both the bacteria and the host. Skin is an effective barrier against bacteria, and this function is partly mediated by the presence of antimicrobial peptides including human cathelicidin peptide LL37. Grain-positive bacteria have been described to have adhesive pili on their surface that mediates specific attachment to the host. Here, we identify, by negative staining transmission electron microscopy (EM), two different types of pilus-like structures commonly expressed on S. epidermidis isolated from newborn infants. We also show that the cathelicidin antimicrobial peptide LL37, constitutively expressed in the skin barrier of the newborn, significantly inhibited growth of S. epidermidis indicating its importance for the ecological stability of the skin microbiota. Further studies are required to elucidate molecular mechanisms of host-microbe interactions, both for the maintenance of a mutually beneficial homeostatic relationship and for the protection of self when it results in overt disease. (Pediatr Res 66: 174-178, 2009)
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| 7. |
- Yu, Jian-Lin, et al.
(författare)
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Fibronectin binding by Propionibacterium acnes
- 1997
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Ingår i: Pathogens and Disease. - 2049-632X. ; 19:3, s. 247-253
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Tidskriftsartikel (refereegranskat)abstract
- Strains of Propionibacterium acnes, isolated from different kinds of orthopaedic and biomaterial-associated infections and from skin flora were shown to express binding of soluble as well as immobilized fibronectin. Among these 7 strains isolated from orthopaedic infections, 2 from breast prostheses, and 9 skin isolates, 2, 2, and 5 strains respectively bound immobilized fibronectin. The fibronectin binding was sensitive to protease and heat treatment, and was inhibited by a cell surface extract from one of the binding strains. In SDS-PAGE and autoradiography of cell surface extracts, a band corresponding to a MW of about 80 kD reacted with fibronectin and the 150 kD fragment of fibronectin. Binding to fibronectin and the 150 kD fragment of fibronectin could be inhibited with heparin. We thus present a first Fn binding protein of P. acnes, a surface exposed protein of 80 kD. None of the strains bound soluble collagen, and only one strain expressed weak binding of vitronectin and bone sialoprotein II.
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