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'''Pleurotolysin''', a sphingomyelin-specific cytolysin consisting of A (17 kDa) and B (59 kDa) components from the [[basidiomycete]] ''Pleurotus ostreatus'', assembles into a transmembrane pore complex. Sakurai et al. 2004 cloned complementary and genomic DNAs encoding pleurotolysin, and studied pore-forming properties of recombinant proteins. Recombinant pleurotolysin A lacking the first methionine was purified as a 17-kDa protein with sphingomyelin-binding activity. The cDNA for pleurotolysin B encoded a precursor consisting of 523 amino acid residues, of which N-terminal 48 amino acid residues were absent in natural pleurotolysin B. Mature and precursor forms of pleurotolysin B were expressed as insoluble 59- and 63-kDa proteins, respectively. Although neither recombinant pleurotolysin A nor B alone was hemolytically active at higher concentrations of up to 100 mg/ml, they cooperatively assembled into a membrane pore complex on human erythrocytes and lysed the cell.
'''Pleurotolysin''', a [[sphingomyelin]]-specific [[cytolysin]] consisting of A (17 kDa) and B (59 kDa) components from the [[basidiomycete]] ''[[Pleurotus ostreatus]]'', assembles into a transmembrane pore complex.<ref name=":0">{{Cite journal|title = Pleurotolysin, a novel sphingomyelin-specific two-component cytolysin from the edible mushroom Pleurotus ostreatus, assembles into a transmembrane pore complex|url = http://www.ncbi.nlm.nih.gov/pubmed/15084605|journal = The Journal of Biological Chemistry|date = 2004-06-25|issn = 0021-9258|pmid = 15084605|pages = 26975–26982|volume = 279|issue = 26|doi = 10.1074/jbc.M402676200|first = Toshio|last = Tomita|first2 = Kayoko|last2 = Noguchi|first3 = Hitomi|last3 = Mimuro|first4 = Fumio|last4 = Ukaji|first5 = Kiyoshi|last5 = Ito|first6 = Noriko|last6 = Sugawara-Tomita|first7 = Yohichi|last7 = Hashimoto}}</ref> The Pleurotolysin Pore-Forming (Pleurotolysin) Family (TC# 1.C.97) is a family of pore forming transporters belonging to the [[MACPF|MACPF superfamily]].


== Research ==
⚫
Tomita et al. 2004 purified pleurotolysin, a sphingomyelin-specific two-component cytolysin from the basidiocarps of Pleurotus ostreatus and studied pore-formation. Pleurotolysin caused leakage of potassium ions from human erythrocytes and formed membrane pores with a functional diameter of 4-5 nm. Pleurotolysin-induced lysis of human erythrocytes was inhibited by the addition of sphingomyelin-cholesterol liposomes to the extracellular space. Pleurotolysin A specifically bound to sphingomyelin-cholesterol liposomes and caused leakage of the internal carboxyfluorescein in concert with pleurotolysin B. Pleurotolysin A and B bound to human erythrocytes in this sequence and assembled into an SDS-stable, 700-kDa complex. Ring-shaped structures with outer and inner diameters of 14 and 7 nm, respectively, were isolated from the solubilized erythrocyte membranes.
Sakurai et al. 2004 cloned complementary and genomic DNAs encoding pleurotolysin, and studied pore-forming properties of recombinant proteins. Recombinant pleurotolysin A lacking the first methionine was purified as a 17-kDa protein with sphingomyelin-binding activity. The cDNA for pleurotolysin B encoded a precursor consisting of 523 amino acid residues, of which N-terminal 48 amino acid residues were absent in natural pleurotolysin B. Mature and precursor forms of pleurotolysin B were expressed as insoluble 59- and 63-kDa proteins, respectively. Although neither recombinant pleurotolysin A nor B alone was hemolytically active at higher concentrations of up to 100 mg/ml, they cooperatively assembled into a membrane pore complex on human erythrocytes and lysed the cell.<ref>{{Cite journal|title = Cloning, expression, and pore-forming properties of mature and precursor forms of pleurotolysin, a sphingomyelin-specific two-component cytolysin from the edible mushroom Pleurotus ostreatus|url = http://www.ncbi.nlm.nih.gov/pubmed/15245918|journal = Biochimica Et Biophysica Acta|date = 2004-07-13|issn = 0006-3002|pmid = 15245918|pages = 65–73|volume = 1679|issue = 1|doi = 10.1016/j.bbaexp.2004.05.002|first = Nobuki|last = Sakurai|first2 = Jun|last2 = Kaneko|first3 = Yoshiyuki|last3 = Kamio|first4 = Toshio|last4 = Tomita}}</ref>


⚫
Tomita et al. 2004 purified pleurotolysin, a sphingomyelin-specific two-component cytolysin from the basidiocarps of ''Pleurotus ostreatus'' and studied pore-formation. Pleurotolysin caused leakage of potassium ions from human erythrocytes and formed membrane pores with a functional diameter of 4-5 nm. Pleurotolysin-induced lysis of human erythrocytes was inhibited by the addition of sphingomyelin-cholesterol liposomes to the extracellular space. Pleurotolysin A specifically bound to sphingomyelin-cholesterol liposomes and caused leakage of the internal carboxyfluorescein in concert with pleurotolysin B. Pleurotolysin A and B bound to human erythrocytes in this sequence and assembled into an SDS-stable, 700-kDa complex. Ring-shaped structures with outer and inner diameters of 14 and 7 nm, respectively, were isolated from the solubilized erythrocyte membranes.<ref name=":0" />
⚫
Another two-component hemolysin, erylysin A and B (EryA and EryB), was isolated from an edible mushroom, Pleurotus eryngii (Shibata et al. 2010). Hemolytic activity was exhibited only by the EryA and EryB mixture. EryA showed one band on SDS-PAGE while EryB showed two bands at 15 kDa (EryB1) and 37 kDa (EryB2). At pH 7.2, EryA exists as a homodimer whereas EryB exists as a heterodimer of B1 and B2. CD spectrum analysis showed T(m) values of 47°C and 37°C for EryA and EryB, respectively. EryB was particularly unstable.


== Homologues ==
While Pleurotolysin B is in the MACPF superfamily (1.C.39), Pleurotolysin A is in the Aegerolysin superfamily. Several members of the Aegerolysin family have been used as tools to detect and visualize ceramide phosphoethanolamine, a major sphingolipid in invertebrates but not in animals (Bhat et al. 2015). It may be distantly related to members of the Equinatoxin Family (1.C.38).
In this TC family, both constituents of pleurotolysin and ostreolysin (A and B) are included under TC#s 1.C.97.1.1 and 1.C.97.1.2, respectively. However, homologues of Pleurotolysin B are found under TC#s 1.C.97.1.3 - 1.9 while homologues of Pleurotolysin A are found under TC#s 1.C.97.2.1 - 2.4 and 3.1 - 3.8. Pleurotolysins A are not homologous to Pleurotolysins B. While some homologues depend on the presence of both constituents for pore formation, as noted for both pleurotolysin and ostreolysin, some homologues of both A and B can form pores without the other. While Pleurotolysin B is in the [[MACPF|MACPF superfamily]] (TC# 1.C.39), Pleurotolysin A is in the Aegerolysin superfamily. Several members of the Aegerolysin family have been used as tools to detect and visualize ceramide phosphoethanolamine, a major sphingolipid in invertebrates but not in animals.<ref>{{Cite journal|title = Evaluation of aegerolysins as novel tools to detect and visualize ceramide phosphoethanolamine, a major sphingolipid in invertebrates|url = http://www.ncbi.nlm.nih.gov/pubmed/26060215|journal = FASEB journal: official publication of the Federation of American Societies for Experimental Biology|date = 2015-09-01|issn = 1530-6860|pmid = 26060215|pages = 3920–3934|volume = 29|issue = 9|doi = 10.1096/fj.15-272112|first = Hema Balakrishna|last = Bhat|first2 = Reiko|last2 = Ishitsuka|first3 = Takehiko|last3 = Inaba|first4 = Motohide|last4 = Murate|first5 = Mitsuhiro|last5 = Abe|first6 = Asami|last6 = Makino|first7 = Ayako|last7 = Kohyama-Koganeya|first8 = Kohjiro|last8 = Nagao|first9 = Atsushi|last9 = Kurahashi}}</ref> It may be distantly related to members of the Equinatoxin Family (TC# 1.C.38).


==== Erylysin ====
⚫
Proteins with membrane-attack complex/perforin (MACPF) domains have a variety of biological roles, including defence and attack, organismal development, and cell adhesion and signalling. The distribution of these proteins in fungi appears to be restricted to some Pezizomycotina and Basidiomycota species only, in correlation with the aegerolysins. These two protein groups coincide in only a few species, and they operate as cytolytic bi-component pore-forming agents (Ota et al. 2014). Representative proteins include pleurotolysin B, which has a MACPF domain, and the aegerolysin-like protein pleurotolysin A, and the very similar ostreolysin A, which have been purified from oyster mushroom (Pleurotus ostreatus). These act in concert to perforate natural and artificial lipid membranes with high cholesterol and sphingomyelin contents. The complex has a 13-meric rosette-like structure with a central lumen that is ~4-5 nm in diameter. The opened transmembrane pore is non-selectively permeable to ions and smaller neutral solutes, and is a cause of cytolysis of a colloid-osmotic type. The biological significance of these proteins for the fungal life-style has been discussed (Ota et al. 2014).
⚫
Another two-component hemolysin, erylysin A and B (EryA and EryB), was isolated from an edible mushroom, ''Pleurotus eryngii''.<ref>{{Cite journal|title = Isolation and characterization of a novel two-component hemolysin, erylysin A and B, from an edible mushroom, Pleurotus eryngii|url = http://www.ncbi.nlm.nih.gov/pubmed/20816689|journal = Toxicon: Official Journal of the International Society on Toxinology|date = 2010-12-01|issn = 1879-3150|pmid = 20816689|pages = 1436–1442|volume = 56|issue = 8|doi = 10.1016/j.toxicon.2010.08.010|first = Taisei|last = Shibata|first2 = Makiko|last2 = Kudou|first3 = Yoshinobu|last3 = Hoshi|first4 = Ayako|last4 = Kudo|first5 = Naoki|last5 = Nanashima|first6 = Kazuo|last6 = Miyairi}}</ref> Hemolytic activity was exhibited only by the EryA and EryB mixture. EryA showed one band on SDS-PAGE while EryB showed two bands at 15 kDa (EryB1) and 37 kDa (EryB2). At pH 7.2, EryA exists as a homodimer whereas EryB exists as a heterodimer of B1 and B2. CD spectrum analysis showed T(m) values of 47°C and 37°C for EryA and EryB, respectively. EryB was particularly unstable.


==== Aegerolysin ====
The aegerolysin family consists of several bacterial and eukaryotic aegerolysin-like proteins. It has been found that aegerolysin and ostreolysin are expressed during formation of primordia and fruiting bodies and possibly play a role in the initial phase of fungal fruiting. The bacterial members of this family are expressed during sporulation. Ostreolysin is cytolytic to various erythrocytes and tumor cells because of pore formation (Berne et al. 2002; Berne et al. 2002; Berne et al. 2009).
The aegerolysin family consists of several bacterial and eukaryotic aegerolysin-like proteins. It has been found that aegerolysin and ostreolysin are expressed during formation of primordia and fruiting bodies and possibly play a role in the initial phase of fungal fruiting. The bacterial members of this family are expressed during sporulation. Ostreolysin is cytolytic to various erythrocytes and tumor cells because of pore formation.<ref>{{Cite journal|title = Pleurotus and Agrocybe hemolysins, new proteins hypothetically involved in fungal fruiting|url = http://www.ncbi.nlm.nih.gov/pubmed/12020804|journal = Biochimica Et Biophysica Acta|date = 2002-04-15|issn = 0006-3002|pmid = 12020804|pages = 153–159|volume = 1570|issue = 3|first = Sabina|last = Berne|first2 = Igor|last2 = Krizaj|first3 = Franc|last3 = Pohleven|first4 = Tom|last4 = Turk|first5 = Peter|last5 = Macek|first6 = Kristina|last6 = Sepcić}}</ref><ref>{{Cite journal|title = Effect of pH on the pore forming activity and conformational stability of ostreolysin, a lipid raft-binding protein from the edible mushroom Pleurotus ostreatus|url = http://www.ncbi.nlm.nih.gov/pubmed/16101298|journal = Biochemistry|date = 2005-08-23|issn = 0006-2960|pmid = 16101298|pages = 11137–11147|volume = 44|issue = 33|doi = 10.1021/bi051013y|first = Sabina|last = Berne|first2 = Kristina|last2 = Sepcić|first3 = Gregor|last3 = Anderluh|first4 = Tom|last4 = Turk|first5 = Peter|last5 = Macek|first6 = Natasa|last6 = Poklar Ulrih}}</ref><ref>{{Cite journal|title = Aegerolysins: structure, function, and putative biological role|url = http://www.ncbi.nlm.nih.gov/pubmed/19309687|journal = Protein Science: A Publication of the Protein Society|date = 2009-04-01|issn = 1469-896X|pmc = 2762582|pmid = 19309687|pages = 694–706|volume = 18|issue = 4|doi = 10.1002/pro.85|first = Sabina|last = Berne|first2 = Ljerka|last2 = Lah|first3 = Kristina|last3 = Sepcić}}</ref>


== Function ==
In this TC family, both constituents of pleurotolysin and ostreolysin (A and B) are included under TC#s 1.C.97.1.1 and 1.2, respectively. However, homologues of Pleurotolysin B are found under TC #s 1.C.97.1.3 - 1.9 while homologues of Pleurotolysin A are found under TC #s 1/C/97.2.1 - 2.4 and 3.1 - 3.8. Pleurotolysins A are not homologous to Pleurotolysins B. While some homologues depend on the presence of both constituents for pore formation, as noted for both pleurotolysin and ostreolysin, some homologues of both A and B can form pores without the other.
⚫
Proteins with membrane-attack complex/perforin (MACPF) domains have a variety of biological roles, including defense and attack, organismal development, and cell adhesion and signaling. The distribution of these proteins in fungi appears to be restricted to some Pezizomycotina and Basidiomycota species only, in correlation with the aegerolysins. These two protein groups coincide in only a few species, and they operate as cytolytic bi-component pore-forming agents.<ref name=":1">{{Cite journal|title = Fungal MACPF-like proteins and aegerolysins: bi-component pore-forming proteins?|url = http://www.ncbi.nlm.nih.gov/pubmed/24798017|journal = Sub-Cellular Biochemistry|date = 2014-01-01|issn = 0306-0225|pmid = 24798017|pages = 271–291|volume = 80|doi = 10.1007/978-94-017-8881-6_14|first = Katja|last = Ota|first2 = Matej|last2 = Butala|first3 = Gabriella|last3 = Viero|first4 = Mauro|last4 = Dalla Serra|first5 = Kristina|last5 = Sepčić|first6 = Peter|last6 = Maček}}</ref> Representative proteins include pleurotolysin B, which has a [[MACPF]] domain, and the aegerolysin-like protein pleurotolysin A, and the very similar ostreolysin A, which have been purified from oyster mushroom (''Pleurotus ostreatus''). These act in concert to perforate natural and artificial lipid membranes with high cholesterol and sphingomyelin contents. The complex has a 13-meric rosette-like structure with a central lumen that is ~ 4-5 nm in diameter. The opened transmembrane pore is non-selectively permeable to ions and smaller neutral solutes, and is a cause of cytolysis of a colloid-osmotic type. The biological significance of these proteins for the fungal life-style has been discussed.<ref name=":1" />

== References ==
{{reflist}}


{{Dual|source=Transporter Classification Database|sourcepath=http://www.tcdb.org/search/result.php?tc=1.C.97|sourcearticle=1.C.97 The Pleurotolysin Pore-Forming (Pleurotolysin) Family|date=20:02, 16 February 2016 (UTC)}}
{{Dual|source=Transporter Classification Database|sourcepath=http://www.tcdb.org/search/result.php?tc=1.C.97|sourcearticle=1.C.97 The Pleurotolysin Pore-Forming (Pleurotolysin) Family|date=20:02, 16 February 2016 (UTC)}}

Revision as of 20:12, 16 February 2016

Pleurotolysin, a sphingomyelin-specific cytolysin consisting of A (17 kDa) and B (59 kDa) components from the basidiomycete Pleurotus ostreatus, assembles into a transmembrane pore complex.[1] The Pleurotolysin Pore-Forming (Pleurotolysin) Family (TC# 1.C.97) is a family of pore forming transporters belonging to the MACPF superfamily.

Research

Sakurai et al. 2004 cloned complementary and genomic DNAs encoding pleurotolysin, and studied pore-forming properties of recombinant proteins. Recombinant pleurotolysin A lacking the first methionine was purified as a 17-kDa protein with sphingomyelin-binding activity. The cDNA for pleurotolysin B encoded a precursor consisting of 523 amino acid residues, of which N-terminal 48 amino acid residues were absent in natural pleurotolysin B. Mature and precursor forms of pleurotolysin B were expressed as insoluble 59- and 63-kDa proteins, respectively. Although neither recombinant pleurotolysin A nor B alone was hemolytically active at higher concentrations of up to 100 mg/ml, they cooperatively assembled into a membrane pore complex on human erythrocytes and lysed the cell.[2]

Tomita et al. 2004 purified pleurotolysin, a sphingomyelin-specific two-component cytolysin from the basidiocarps of Pleurotus ostreatus and studied pore-formation. Pleurotolysin caused leakage of potassium ions from human erythrocytes and formed membrane pores with a functional diameter of 4-5 nm. Pleurotolysin-induced lysis of human erythrocytes was inhibited by the addition of sphingomyelin-cholesterol liposomes to the extracellular space. Pleurotolysin A specifically bound to sphingomyelin-cholesterol liposomes and caused leakage of the internal carboxyfluorescein in concert with pleurotolysin B. Pleurotolysin A and B bound to human erythrocytes in this sequence and assembled into an SDS-stable, 700-kDa complex. Ring-shaped structures with outer and inner diameters of 14 and 7 nm, respectively, were isolated from the solubilized erythrocyte membranes.[1]

Homologues

In this TC family, both constituents of pleurotolysin and ostreolysin (A and B) are included under TC#s 1.C.97.1.1 and 1.C.97.1.2, respectively. However, homologues of Pleurotolysin B are found under TC#s 1.C.97.1.3 - 1.9 while homologues of Pleurotolysin A are found under TC#s 1.C.97.2.1 - 2.4 and 3.1 - 3.8. Pleurotolysins A are not homologous to Pleurotolysins B. While some homologues depend on the presence of both constituents for pore formation, as noted for both pleurotolysin and ostreolysin, some homologues of both A and B can form pores without the other. While Pleurotolysin B is in the MACPF superfamily (TC# 1.C.39), Pleurotolysin A is in the Aegerolysin superfamily. Several members of the Aegerolysin family have been used as tools to detect and visualize ceramide phosphoethanolamine, a major sphingolipid in invertebrates but not in animals.[3] It may be distantly related to members of the Equinatoxin Family (TC# 1.C.38).

Erylysin

Another two-component hemolysin, erylysin A and B (EryA and EryB), was isolated from an edible mushroom, Pleurotus eryngii.[4] Hemolytic activity was exhibited only by the EryA and EryB mixture. EryA showed one band on SDS-PAGE while EryB showed two bands at 15 kDa (EryB1) and 37 kDa (EryB2). At pH 7.2, EryA exists as a homodimer whereas EryB exists as a heterodimer of B1 and B2. CD spectrum analysis showed T(m) values of 47°C and 37°C for EryA and EryB, respectively. EryB was particularly unstable.

Aegerolysin

The aegerolysin family consists of several bacterial and eukaryotic aegerolysin-like proteins. It has been found that aegerolysin and ostreolysin are expressed during formation of primordia and fruiting bodies and possibly play a role in the initial phase of fungal fruiting. The bacterial members of this family are expressed during sporulation. Ostreolysin is cytolytic to various erythrocytes and tumor cells because of pore formation.[5][6][7]

Function

Proteins with membrane-attack complex/perforin (MACPF) domains have a variety of biological roles, including defense and attack, organismal development, and cell adhesion and signaling. The distribution of these proteins in fungi appears to be restricted to some Pezizomycotina and Basidiomycota species only, in correlation with the aegerolysins. These two protein groups coincide in only a few species, and they operate as cytolytic bi-component pore-forming agents.[8] Representative proteins include pleurotolysin B, which has a MACPF domain, and the aegerolysin-like protein pleurotolysin A, and the very similar ostreolysin A, which have been purified from oyster mushroom (Pleurotus ostreatus). These act in concert to perforate natural and artificial lipid membranes with high cholesterol and sphingomyelin contents. The complex has a 13-meric rosette-like structure with a central lumen that is ~ 4-5 nm in diameter. The opened transmembrane pore is non-selectively permeable to ions and smaller neutral solutes, and is a cause of cytolysis of a colloid-osmotic type. The biological significance of these proteins for the fungal life-style has been discussed.[8]

References

  1. ^ a b Tomita, Toshio; Noguchi, Kayoko; Mimuro, Hitomi; Ukaji, Fumio; Ito, Kiyoshi; Sugawara-Tomita, Noriko; Hashimoto, Yohichi (2004-06-25). "Pleurotolysin, a novel sphingomyelin-specific two-component cytolysin from the edible mushroom Pleurotus ostreatus, assembles into a transmembrane pore complex". The Journal of Biological Chemistry. 279 (26): 26975–26982. doi:10.1074/jbc.M402676200. ISSN 0021-9258. PMID 15084605.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  2. ^ Sakurai, Nobuki; Kaneko, Jun; Kamio, Yoshiyuki; Tomita, Toshio (2004-07-13). "Cloning, expression, and pore-forming properties of mature and precursor forms of pleurotolysin, a sphingomyelin-specific two-component cytolysin from the edible mushroom Pleurotus ostreatus". Biochimica Et Biophysica Acta. 1679 (1): 65–73. doi:10.1016/j.bbaexp.2004.05.002. ISSN 0006-3002. PMID 15245918.
  3. ^ Bhat, Hema Balakrishna; Ishitsuka, Reiko; Inaba, Takehiko; Murate, Motohide; Abe, Mitsuhiro; Makino, Asami; Kohyama-Koganeya, Ayako; Nagao, Kohjiro; Kurahashi, Atsushi (2015-09-01). "Evaluation of aegerolysins as novel tools to detect and visualize ceramide phosphoethanolamine, a major sphingolipid in invertebrates". FASEB journal: official publication of the Federation of American Societies for Experimental Biology. 29 (9): 3920–3934. doi:10.1096/fj.15-272112. ISSN 1530-6860. PMID 26060215.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  4. ^ Shibata, Taisei; Kudou, Makiko; Hoshi, Yoshinobu; Kudo, Ayako; Nanashima, Naoki; Miyairi, Kazuo (2010-12-01). "Isolation and characterization of a novel two-component hemolysin, erylysin A and B, from an edible mushroom, Pleurotus eryngii". Toxicon: Official Journal of the International Society on Toxinology. 56 (8): 1436–1442. doi:10.1016/j.toxicon.2010.08.010. ISSN 1879-3150. PMID 20816689.
  5. ^ Berne, Sabina; Krizaj, Igor; Pohleven, Franc; Turk, Tom; Macek, Peter; Sepcić, Kristina (2002-04-15). "Pleurotus and Agrocybe hemolysins, new proteins hypothetically involved in fungal fruiting". Biochimica Et Biophysica Acta. 1570 (3): 153–159. ISSN 0006-3002. PMID 12020804.
  6. ^ Berne, Sabina; Sepcić, Kristina; Anderluh, Gregor; Turk, Tom; Macek, Peter; Poklar Ulrih, Natasa (2005-08-23). "Effect of pH on the pore forming activity and conformational stability of ostreolysin, a lipid raft-binding protein from the edible mushroom Pleurotus ostreatus". Biochemistry. 44 (33): 11137–11147. doi:10.1021/bi051013y. ISSN 0006-2960. PMID 16101298.
  7. ^ Berne, Sabina; Lah, Ljerka; Sepcić, Kristina (2009-04-01). "Aegerolysins: structure, function, and putative biological role". Protein Science: A Publication of the Protein Society. 18 (4): 694–706. doi:10.1002/pro.85. ISSN 1469-896X. PMC 2762582. PMID 19309687.
  8. ^ a b Ota, Katja; Butala, Matej; Viero, Gabriella; Dalla Serra, Mauro; Sepčić, Kristina; Maček, Peter (2014-01-01). "Fungal MACPF-like proteins and aegerolysins: bi-component pore-forming proteins?". Sub-Cellular Biochemistry. 80: 271–291. doi:10.1007/978-94-017-8881-6_14. ISSN 0306-0225. PMID 24798017.

As of 20:02, 16 February 2016 (UTC), this article is derived in whole or in part from Transporter Classification Database. The copyright holder has licensed the content in a manner that permits reuse under CC BY-SA 3.0 and GFDL. All relevant terms must be followed. The original text was at "1.C.97 The Pleurotolysin Pore-Forming (Pleurotolysin) Family"

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