Erysipelas pathophysiology: Difference between revisions
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**[[Epidermal]] damages, including [[abrasions]] or [[lesions]], allow the pathogen to adhere without being removed by natural [[exfoliation]]. | **[[Epidermal]] 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]]: | **''[[Streptococcus pyogenes]]'' adheres to the [[dermis]] due to the following [[virulence factors]]: | ||
***Containing [[M protein]], allowing colonization | ***Containing [[M protein]], allowing colonization<ref name="pmid4564883">{{cite journal |vauthors=Ellen RP, Gibbons RJ |title=M protein-associated adherence of Streptococcus pyogenes to epithelial surfaces: prerequisite for virulence |journal=Infect. Immun. |volume=5 |issue=5 |pages=826–30 |year=1972 |pmid=4564883 |pmc=422446 |doi= |url=}}</ref> | ||
***[[Lipotechoic acid]] (LTA): binds with [[fibronectin]] or [[fibrinogen]], causing adhesion of the bacteria to the [[dermis]] | ***[[Lipotechoic acid]] (LTA): binds with [[fibronectin]] or [[fibrinogen]], causing adhesion of the bacteria to the [[dermis]]<ref name="pmid8063411">{{cite journal |vauthors=Courtney HS, Li Y, Dale JB, Hasty DL |title=Cloning, sequencing, and expression of a fibronectin/fibrinogen-binding protein from group A streptococci |journal=Infect. Immun. |volume=62 |issue=9 |pages=3937–46 |year=1994 |pmid=8063411 |pmc=303051 |doi= |url=}}</ref> | ||
***[[Protein]] F: binds with [[fibronectin]] to mediate adhesion | ***[[Protein]] F: binds with [[fibronectin]] to mediate adhesion<ref name="pmid1385871">{{cite journal |vauthors=Hanski E, Caparon M |title=Protein F, a fibronectin-binding protein, is an adhesin of the group A streptococcus Streptococcus pyogenes |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue=13 |pages=6172–6 |year=1992 |pmid=1385871 |pmc=402144 |doi= |url=}}</ref> | ||
***29-kDa [[fibronectin]]-binding [[protein]] | ***29-kDa [[fibronectin]]-binding [[protein]]<ref name="CourtneyHasty1992">{{cite journal|last1=Courtney|first1=Harry S.|last2=Hasty|first2=David L.|last3=Dale|first3=James B.|last4=Poirier|first4=Thomas P.|title=A 28-kilodalton fibronectin-binding protein of group a streptococci|journal=Current Microbiology|volume=25|issue=5|year=1992|pages=245–250|issn=0343-8651|doi=10.1007/BF01575856}}</ref> | ||
***[[Glyceraldehyde 3-phosphate dehydrogenase]]<ref name="pmid8760943">{{cite journal |vauthors=Winram SB, Lottenberg R |title=The plasmin-binding protein Plr of group A streptococci is identified as glyceraldehyde-3-phosphate dehydrogenase |journal=Microbiology (Reading, Engl.) |volume=142 ( Pt 8) |issue= |pages=2311–20 |year=1996 |pmid=8760943 |doi=10.1099/13500872-142-8-2311 |url=}}</ref> | ***[[Glyceraldehyde 3-phosphate dehydrogenase]]<ref name="pmid8760943">{{cite journal |vauthors=Winram SB, Lottenberg R |title=The plasmin-binding protein Plr of group A streptococci is identified as glyceraldehyde-3-phosphate dehydrogenase |journal=Microbiology (Reading, Engl.) |volume=142 ( Pt 8) |issue= |pages=2311–20 |year=1996 |pmid=8760943 |doi=10.1099/13500872-142-8-2311 |url=}}</ref> | ||
***70-kDa [[galactose]]-binding [[protein]] | ***70-kDa [[galactose]]-binding [[protein]]<ref name="WalströmTylewska1982">{{cite journal|last1=Walström|first1=Torkel|last2=Tylewska|first2=Stanislawa|title=Glycoconjugates as possible receptors forStreptococcus pyogenes|journal=Current Microbiology|volume=7|issue=6|year=1982|pages=343–346|issn=0343-8651|doi=10.1007/BF01572601}}</ref> | ||
***[[Vitronectin]]-binding S [[protein]]<ref name="pmid2459063">{{cite journal |vauthors=Valentin-Weigand P, Grulich-Henn J, Chhatwal GS, Müller-Berghaus G, Blobel H, Preissner KT |title=Mediation of adherence of streptococci to human endothelial cells by complement S protein (vitronectin) |journal=Infect. Immun. |volume=56 |issue=11 |pages=2851–5 |year=1988 |pmid=2459063 |pmc=259660 |doi= |url=}}</ref> | ***[[Vitronectin]]-binding S [[protein]]<ref name="pmid2459063">{{cite journal |vauthors=Valentin-Weigand P, Grulich-Henn J, Chhatwal GS, Müller-Berghaus G, Blobel H, Preissner KT |title=Mediation of adherence of streptococci to human endothelial cells by complement S protein (vitronectin) |journal=Infect. Immun. |volume=56 |issue=11 |pages=2851–5 |year=1988 |pmid=2459063 |pmc=259660 |doi= |url=}}</ref> | ||
***[[Collagen]]-binding protein<ref name="pmid7814395">{{cite journal |vauthors=Visai L, Bozzini S, Raucci G, Toniolo A, Speziale P |title=Isolation and characterization of a novel collagen-binding protein from Streptococcus pyogenes strain 6414 |journal=J. Biol. Chem. |volume=270 |issue=1 |pages=347–53 |year=1995 |pmid=7814395 |doi= |url=}}</ref> | ***[[Collagen]]-binding protein<ref name="pmid7814395">{{cite journal |vauthors=Visai L, Bozzini S, Raucci G, Toniolo A, Speziale P |title=Isolation and characterization of a novel collagen-binding protein from Streptococcus pyogenes strain 6414 |journal=J. Biol. Chem. |volume=270 |issue=1 |pages=347–53 |year=1995 |pmid=7814395 |doi= |url=}}</ref> | ||
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**Upon adhesion, ''[[Streptococcus pyogenes]]'' begin to invade through expression of [[M protein]] or [[fibronectin]]-binding [[protein]]. | **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]].<ref name="pmid2964038">{{cite journal |vauthors=Horstmann RD, Sievertsen HJ, Knobloch J, Fischetti VA |title=Antiphagocytic activity of streptococcal M protein: selective binding of complement control protein factor H |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=85 |issue=5 |pages=1657–61 |year=1988 |pmid=2964038 |pmc=279833 |doi= |url=}}</ref><ref name="pmid7042754">{{cite journal |vauthors=Whitnack E, Beachey EH |title=Antiopsonic activity of fibrinogen bound to M protein on the surface of group A streptococci |journal=J. Clin. Invest. |volume=69 |issue=4 |pages=1042–5 |year=1982 |pmid=7042754 |pmc=370160 |doi= |url=}}</ref> | **[[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]].<ref name="pmid2964038">{{cite journal |vauthors=Horstmann RD, Sievertsen HJ, Knobloch J, Fischetti VA |title=Antiphagocytic activity of streptococcal M protein: selective binding of complement control protein factor H |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=85 |issue=5 |pages=1657–61 |year=1988 |pmid=2964038 |pmc=279833 |doi= |url=}}</ref><ref name="pmid7042754">{{cite journal |vauthors=Whitnack E, Beachey EH |title=Antiopsonic activity of fibrinogen bound to M protein on the surface of group A streptococci |journal=J. Clin. Invest. |volume=69 |issue=4 |pages=1042–5 |year=1982 |pmid=7042754 |pmc=370160 |doi= |url=}}</ref> | ||
**Colonization of the [[bacteria]] begins; | **Colonization of the [[bacteria]] begins; erysipelas develops from the [[inflammatory]] response of the increased volume of [[leukocytes]] at the point of infection. | ||
**The [[streptococcal]] pyrogenic [[exotoxins]] release large amounts of [[cytokines]] that result in tissue damage characteristic of | **The [[streptococcal]] pyrogenic [[exotoxins]] release large amounts of [[cytokines]] that result in tissue damage characteristic of erysipelas.<ref name="pmid10816507">{{cite journal |vauthors=Chatellier S, Ihendyane N, Kansal RG, Khambaty F, Basma H, Norrby-Teglund A, Low DE, McGeer A, Kotb M |title=Genetic relatedness and superantigen expression in group A streptococcus serotype M1 isolates from patients with severe and nonsevere invasive diseases |journal=Infect. Immun. |volume=68 |issue=6 |pages=3523–34 |year=2000 |pmid=10816507 |pmc=97638 |doi= |url=}}</ref> | ||
==Genetics== | ==Genetics== | ||
There is evidence of increased susceptibility to | There is evidence of increased susceptibility to erysipelas in individuals with [[streptococcal infection]], due to the following genetic factors:<ref name="pmid23437094">{{cite journal |vauthors=Hannula-Jouppi K, Massinen S, Siljander T, Mäkelä S, Kivinen K, Leinonen R, Jiao H, Aitos P, Karppelin M, Vuopio J, Syrjänen J, Kere J |title=Genetic susceptibility to non-necrotizing erysipelas/cellulitis |journal=PLoS ONE |volume=8 |issue=2 |pages=e56225 |year=2013 |pmid=23437094 |pmc=3577772 |doi=10.1371/journal.pone.0056225 |url=}}</ref> | ||
*[[Human leukocyte antigen]] (HLA) Class II and T-cell receptor Vβ variation can cause differing susceptibility due to their influence on Super antigen production, contributing the to severity of [[cytokine]] release from [[inflammation]].<ref name="pmid10816507">{{cite journal |vauthors=Chatellier S, Ihendyane N, Kansal RG, Khambaty F, Basma H, Norrby-Teglund A, Low DE, McGeer A, Kotb M |title=Genetic relatedness and superantigen expression in group A streptococcus serotype M1 isolates from patients with severe and nonsevere invasive diseases |journal=Infect. Immun. |volume=68 |issue=6 |pages=3523–34 |year=2000 |pmid=10816507 |pmc=97638 |doi= |url=}}</ref> | *[[Human leukocyte antigen]] (HLA) Class II and T-cell receptor Vβ variation can cause differing susceptibility due to their influence on Super antigen production, contributing the to severity of [[cytokine]] release from [[inflammation]].<ref name="pmid10816507">{{cite journal |vauthors=Chatellier S, Ihendyane N, Kansal RG, Khambaty F, Basma H, Norrby-Teglund A, Low DE, McGeer A, Kotb M |title=Genetic relatedness and superantigen expression in group A streptococcus serotype M1 isolates from patients with severe and nonsevere invasive diseases |journal=Infect. Immun. |volume=68 |issue=6 |pages=3523–34 |year=2000 |pmid=10816507 |pmc=97638 |doi= |url=}}</ref> | ||
*The region [[Angiotensin II receptory type 1]] (AGRT1) on the [[chromosome]] 3q22 has been | *The region [[Angiotensin II receptory type 1]] (AGRT1) on the [[chromosome]] 3q22 has been shown to reveal susceptibility to developing erysipelas by determining an individual's [[cytokine]] response to ''[[Streptococcus pyogenes]]'' infection.<ref name="pmid23437094">{{cite journal |vauthors=Hannula-Jouppi K, Massinen S, Siljander T, Mäkelä S, Kivinen K, Leinonen R, Jiao H, Aitos P, Karppelin M, Vuopio J, Syrjänen J, Kere J |title=Genetic susceptibility to non-necrotizing erysipelas/cellulitis |journal=PLoS ONE |volume=8 |issue=2 |pages=e56225 |year=2013 |pmid=23437094 |pmc=3577772 |doi=10.1371/journal.pone.0056225 |url=}}</ref> | ||
==Associated Conditions== | ==Associated Conditions== | ||
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> | 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> | ||
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==References== | ==References== | ||
{{Reflist|2}} | {{Reflist|2}} | ||
{{WH}} | {{WH}} | ||
{{WS}} | {{WS}} | ||
[[Category:Dermatology]] | |||
[[Category:FinalQCRequired]] | |||
[[Category:Emergency medicine]] | |||
[[Category:Disease]] | |||
[[Category:Up-To-Date]] | |||
[[Category:Infectious disease]] | |||
Latest revision as of 21:39, 29 July 2020
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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
Erysipelas develops from epidermal penetration of streptococcal bacteria, usually the group A streptococcus Streptococcus pyogenes.The 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. A myriad of virulence factors causes bacteria to adhere to the dermis. 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. Colonization of the bacteria begins; erysipelas develops from the inflammatory response of the increased volume of leukocytes at the point of infection. The streptococcal pyrogenic exotoxins release large amounts of cytokines that result in tissue damage characteristic of erysipelas. There is evidence of genetic predisposition and susceptibility to erysipelas in individuals with streptococcal infection. Erysipelas is associated with the following conditions associated with group A streptococcal infection, including cellulitis, necrotizing fasciitis, and toxic shock syndrome.
Pathogenesis
Erysipelas develops from exotoxins released due to 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.
- Epidermal 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.
- The streptococcal pyrogenic exotoxins release large amounts of cytokines that result in tissue damage characteristic of erysipelas.[13]
Genetics
There is evidence of increased susceptibility to erysipelas in individuals with streptococcal infection, due to the following genetic factors:[14]
- Human leukocyte antigen (HLA) Class II and T-cell receptor Vβ variation can cause differing susceptibility due to their influence on Super antigen production, contributing the to severity of cytokine release from inflammation.[13]
- The region Angiotensin II receptory type 1 (AGRT1) on the chromosome 3q22 has been shown to reveal susceptibility to developing erysipelas by determining an individual's cytokine response to Streptococcus pyogenes infection.[14]
Associated Conditions
Erysipelas is associated with the following streptococcal conditions:[15]
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.
- ↑ 13.0 13.1 Chatellier S, Ihendyane N, Kansal RG, Khambaty F, Basma H, Norrby-Teglund A, Low DE, McGeer A, Kotb M (2000). "Genetic relatedness and superantigen expression in group A streptococcus serotype M1 isolates from patients with severe and nonsevere invasive diseases". Infect. Immun. 68 (6): 3523–34. PMC 97638. PMID 10816507.
- ↑ 14.0 14.1 Hannula-Jouppi K, Massinen S, Siljander T, Mäkelä S, Kivinen K, Leinonen R, Jiao H, Aitos P, Karppelin M, Vuopio J, Syrjänen J, Kere J (2013). "Genetic susceptibility to non-necrotizing erysipelas/cellulitis". PLoS ONE. 8 (2): e56225. doi:10.1371/journal.pone.0056225. PMC 3577772. PMID 23437094.
- ↑ 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.