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Vitellogenin functions as a multivalent pattern recognition receptor with an opsonic activity.

Li Z, Zhang S, Liu Q - PLoS ONE (2008)

Bottom Line: Vitellogenin (Vg), a major reproductive protein, has been associated with infection-resistant response in fish.This study shows that fish Vg plays an integrative function in regulating immunity via its pleiotropic effects on both recognizing pathogen-associated molecular patterns and promoting macrophage phagocytosis.It also supports the notion that factors normally involved in control of female reproduction are associated with immunity in organisms that rely on Vg for oocyte development.

View Article: PubMed Central - PubMed

Affiliation: Department of Marine Biology, Ocean University of China, Qingdao, People's Republic of China.

ABSTRACT

Background: Vitellogenin (Vg), a major reproductive protein, has been associated with infection-resistant response in fish. However, the underlying mechanisms by which Vg is involved in anti-infectious response are not understood.

Methodology/results: By both protein-microbe interaction analysis and enzyme-linked immunosorbent assay as well as phagocytosis test, we demonstrate for the first time that fish Vg acts as a pattern recognition molecule with multiple specificities that can recognize bacteria as well as fungus rather than self components from fish, and functions as an opsonin that can enhance macrophage phagocytosis.

Conclusions: This study shows that fish Vg plays an integrative function in regulating immunity via its pleiotropic effects on both recognizing pathogen-associated molecular patterns and promoting macrophage phagocytosis. It also supports the notion that factors normally involved in control of female reproduction are associated with immunity in organisms that rely on Vg for oocyte development.

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Binding of Vg to various ligands.LPS, LTA, PGN, laminarin and β-1,3-glucan dissolved in re-distilled water were applied to a 96-well microplate, and air-dried overnight at room temperature, followed by ELISA. BSA, serum proteins (SPs) and total muscle proteins (TMPs) of H. otakii at the same concentrations were treated similarly as controls. Data were expressed as mean values±SEM (n = 3). The bars represent the standard error of mean values. Although Vg slightly binds to BSA and SPs and TMPs of H. otakii, its affinity to the immobilized ligands is significantly higher (p<0.05). (A–E) Binding of Vg to LPS, LTA, PGN, β-1,3-glucan and laminarin.
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pone-0001940-g003: Binding of Vg to various ligands.LPS, LTA, PGN, laminarin and β-1,3-glucan dissolved in re-distilled water were applied to a 96-well microplate, and air-dried overnight at room temperature, followed by ELISA. BSA, serum proteins (SPs) and total muscle proteins (TMPs) of H. otakii at the same concentrations were treated similarly as controls. Data were expressed as mean values±SEM (n = 3). The bars represent the standard error of mean values. Although Vg slightly binds to BSA and SPs and TMPs of H. otakii, its affinity to the immobilized ligands is significantly higher (p<0.05). (A–E) Binding of Vg to LPS, LTA, PGN, β-1,3-glucan and laminarin.

Mentions: To better understand the mechanisms of binding activity, an enzyme-linked immunosorbent assay (ELISA) was carried out to investigate what molecules on the microbial surfaces are recognized by Vg. Although Vg slightly bound to BSA, it had a significantly stronger affinity to the immobilized ligands including LPS from Gram-negative bacteria, LTA from Gram-positive bacteria, PGN from both Gram-positive and Gram-negative bacteria, β-1,3-glucan from fungi and laminarin from brown algae (p<0.05; Fig. 3). Moreover, the affinity of Vg to the serum proteins (SPs) and total muscle proteins (TMPs) extracted from H. otakii itself was also markedly lower than that of Vg binding to the immobilized ligands (p<0.05). These demonstrated that Vg possesses a significantly higher affinity to the microbial surface molecules rather than BSA and the self components from H. otakii itself.


Vitellogenin functions as a multivalent pattern recognition receptor with an opsonic activity.

Li Z, Zhang S, Liu Q - PLoS ONE (2008)

Binding of Vg to various ligands.LPS, LTA, PGN, laminarin and β-1,3-glucan dissolved in re-distilled water were applied to a 96-well microplate, and air-dried overnight at room temperature, followed by ELISA. BSA, serum proteins (SPs) and total muscle proteins (TMPs) of H. otakii at the same concentrations were treated similarly as controls. Data were expressed as mean values±SEM (n = 3). The bars represent the standard error of mean values. Although Vg slightly binds to BSA and SPs and TMPs of H. otakii, its affinity to the immobilized ligands is significantly higher (p<0.05). (A–E) Binding of Vg to LPS, LTA, PGN, β-1,3-glucan and laminarin.
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Related In: Results  -  Collection

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getmorefigures.php?uid=PMC2277463&req=5

pone-0001940-g003: Binding of Vg to various ligands.LPS, LTA, PGN, laminarin and β-1,3-glucan dissolved in re-distilled water were applied to a 96-well microplate, and air-dried overnight at room temperature, followed by ELISA. BSA, serum proteins (SPs) and total muscle proteins (TMPs) of H. otakii at the same concentrations were treated similarly as controls. Data were expressed as mean values±SEM (n = 3). The bars represent the standard error of mean values. Although Vg slightly binds to BSA and SPs and TMPs of H. otakii, its affinity to the immobilized ligands is significantly higher (p<0.05). (A–E) Binding of Vg to LPS, LTA, PGN, β-1,3-glucan and laminarin.
Mentions: To better understand the mechanisms of binding activity, an enzyme-linked immunosorbent assay (ELISA) was carried out to investigate what molecules on the microbial surfaces are recognized by Vg. Although Vg slightly bound to BSA, it had a significantly stronger affinity to the immobilized ligands including LPS from Gram-negative bacteria, LTA from Gram-positive bacteria, PGN from both Gram-positive and Gram-negative bacteria, β-1,3-glucan from fungi and laminarin from brown algae (p<0.05; Fig. 3). Moreover, the affinity of Vg to the serum proteins (SPs) and total muscle proteins (TMPs) extracted from H. otakii itself was also markedly lower than that of Vg binding to the immobilized ligands (p<0.05). These demonstrated that Vg possesses a significantly higher affinity to the microbial surface molecules rather than BSA and the self components from H. otakii itself.

Bottom Line: Vitellogenin (Vg), a major reproductive protein, has been associated with infection-resistant response in fish.This study shows that fish Vg plays an integrative function in regulating immunity via its pleiotropic effects on both recognizing pathogen-associated molecular patterns and promoting macrophage phagocytosis.It also supports the notion that factors normally involved in control of female reproduction are associated with immunity in organisms that rely on Vg for oocyte development.

View Article: PubMed Central - PubMed

Affiliation: Department of Marine Biology, Ocean University of China, Qingdao, People's Republic of China.

ABSTRACT

Background: Vitellogenin (Vg), a major reproductive protein, has been associated with infection-resistant response in fish. However, the underlying mechanisms by which Vg is involved in anti-infectious response are not understood.

Methodology/results: By both protein-microbe interaction analysis and enzyme-linked immunosorbent assay as well as phagocytosis test, we demonstrate for the first time that fish Vg acts as a pattern recognition molecule with multiple specificities that can recognize bacteria as well as fungus rather than self components from fish, and functions as an opsonin that can enhance macrophage phagocytosis.

Conclusions: This study shows that fish Vg plays an integrative function in regulating immunity via its pleiotropic effects on both recognizing pathogen-associated molecular patterns and promoting macrophage phagocytosis. It also supports the notion that factors normally involved in control of female reproduction are associated with immunity in organisms that rely on Vg for oocyte development.

Show MeSH