Erysipelas pathophysiology: Difference between revisions
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==Associated Conditions== | ==Associated Conditions== | ||
Erysipelas is associated with the following [[streptococcal]] | Erysipelas is associated with the following [[streptococcal]] conditions:<ref name="BisnoStevens1996">{{cite journal|last1=Bisno|first1=Alan L.|last2=Stevens|first2=Dennis L.|title=Streptococcal Infections of Skin and Soft Tissues|journal=New England Journal of Medicine|volume=334|issue=4|year=1996|pages=240–246|issn=0028-4793|doi=10.1056/NEJM199601253340407}}</ref> | ||
*[[Cellulitis]] | *[[Cellulitis]] | ||
*[[Necrotizing fasciitis]] | *[[Necrotizing fasciitis]] | ||
*[[Toxic shock syndrome]] | |||
==References== | ==References== | ||
Revision as of 14:27, 9 September 2016
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Erysipelas Microchapters |
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Editor-In-Chief: C. Michael Gibson, M.S., M.D. [1]; Associate Editor(s)-in-Chief: Luke Rusowicz-Orazem, B.S.
Overview
Historically, the face was most affected; today the legs are affected most often. Erysipelas infections can enter the skin through minor trauma, eczema, surgical incisions and ulcers, and often originate from strep bacteria in the subject's own nasal passages.
Pathogenesis
Erysipelas develops from epidermal penetration of the pathogenic bacteria.
- Group A streptococcal infection causes Erysipelas upon infiltration of the epidermis through a skin abrasion or lesion.[1]
- The streptococcal infection occurs upon the binding of superficial ligands to the epidermal receptor cells.
- Dermal damages, including abrasions or lesions, allow the pathogen to adhere without being removed by natural exfoliation.
- Streptococcus pyogenes adheres to the dermis due to the following virulence factors:
- Containing M protein, allowing colonization.[2]
- Lipotechoic acid (LTA): binds with fibronectin or fibrinogen, causing adhesion of the bacteria to the dermis.[3]
- Protein F: binds with fibronectin to mediate adhesion.[4]
- 29-kDa fibronectin-binding protein.[5]
- Glyceraldehyde 3-phosphate dehydrogenase[6]
- 70-kDa galactose-binding protein.[7]
- Vitronectin-binding S protein[8]
- Collagen-binding protein[9]
- Serum opacity factor
- Hyaluronate capsule[10]
- Upon adhesion, Streptococcus pyogenes begin to invade through expression of M protein or fibronectin-binding protein.
- Phagocytosis is inhibited by the bacteria due to the binding of factor H and the binding of fibrinogen on the surface of the M protein.[11][12]
- Colonization of the bacteria begins; Erysipelas develops from the inflammatory response of the increased volume of leukocytes at the point of infection.
Associated Conditions
Erysipelas is associated with the following streptococcal conditions:[13]
References
- ↑ Cunningham, M. W. (2000). "Pathogenesis of Group A Streptococcal Infections". Clinical Microbiology Reviews. 13 (3): 470–511. doi:10.1128/CMR.13.3.470-511.2000. ISSN 0893-8512.
- ↑ Ellen RP, Gibbons RJ (1972). "M protein-associated adherence of Streptococcus pyogenes to epithelial surfaces: prerequisite for virulence". Infect. Immun. 5 (5): 826–30. PMC 422446. PMID 4564883.
- ↑ Courtney HS, Li Y, Dale JB, Hasty DL (1994). "Cloning, sequencing, and expression of a fibronectin/fibrinogen-binding protein from group A streptococci". Infect. Immun. 62 (9): 3937–46. PMC 303051. PMID 8063411.
- ↑ Hanski E, Caparon M (1992). "Protein F, a fibronectin-binding protein, is an adhesin of the group A streptococcus Streptococcus pyogenes". Proc. Natl. Acad. Sci. U.S.A. 89 (13): 6172–6. PMC 402144. PMID 1385871.
- ↑ Courtney, Harry S.; Hasty, David L.; Dale, James B.; Poirier, Thomas P. (1992). "A 28-kilodalton fibronectin-binding protein of group a streptococci". Current Microbiology. 25 (5): 245–250. doi:10.1007/BF01575856. ISSN 0343-8651.
- ↑ Winram SB, Lottenberg R (1996). "The plasmin-binding protein Plr of group A streptococci is identified as glyceraldehyde-3-phosphate dehydrogenase". Microbiology (Reading, Engl.). 142 ( Pt 8): 2311–20. doi:10.1099/13500872-142-8-2311. PMID 8760943.
- ↑ Walström, Torkel; Tylewska, Stanislawa (1982). "Glycoconjugates as possible receptors forStreptococcus pyogenes". Current Microbiology. 7 (6): 343–346. doi:10.1007/BF01572601. ISSN 0343-8651.
- ↑ Valentin-Weigand P, Grulich-Henn J, Chhatwal GS, Müller-Berghaus G, Blobel H, Preissner KT (1988). "Mediation of adherence of streptococci to human endothelial cells by complement S protein (vitronectin)". Infect. Immun. 56 (11): 2851–5. PMC 259660. PMID 2459063.
- ↑ Visai L, Bozzini S, Raucci G, Toniolo A, Speziale P (1995). "Isolation and characterization of a novel collagen-binding protein from Streptococcus pyogenes strain 6414". J. Biol. Chem. 270 (1): 347–53. PMID 7814395.
- ↑ Wessels MR, Bronze MS (1994). "Critical role of the group A streptococcal capsule in pharyngeal colonization and infection in mice". Proc. Natl. Acad. Sci. U.S.A. 91 (25): 12238–42. PMC 45412. PMID 7991612.
- ↑ Horstmann RD, Sievertsen HJ, Knobloch J, Fischetti VA (1988). "Antiphagocytic activity of streptococcal M protein: selective binding of complement control protein factor H". Proc. Natl. Acad. Sci. U.S.A. 85 (5): 1657–61. PMC 279833. PMID 2964038.
- ↑ Whitnack E, Beachey EH (1982). "Antiopsonic activity of fibrinogen bound to M protein on the surface of group A streptococci". J. Clin. Invest. 69 (4): 1042–5. PMC 370160. PMID 7042754.
- ↑ Bisno, Alan L.; Stevens, Dennis L. (1996). "Streptococcal Infections of Skin and Soft Tissues". New England Journal of Medicine. 334 (4): 240–246. doi:10.1056/NEJM199601253340407. ISSN 0028-4793.