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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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Purification and identification of Vg.(A) Purification of Vg and determination of carbohydrate, lipid and phosphorus components. The proteins were run on a 7.5% native PAGE. lane 1, marker; lane 2, plasma (diluted 20-fold) of fish injected with E2; lane 3, plasma (diluted 20-fold) of fish injected with 0.9% NaCl; lane 4, purified Vg; lanes 5, 6 and 7, purified Vg stained with Schiff reagent, methyl green and Sudan black B, respectively. The protein induced by E2 stained positive for carbohydrate, lipid, and phosphorus. (B) Peptide mass mapping of the purified protein.
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pone-0001940-g001: Purification and identification of Vg.(A) Purification of Vg and determination of carbohydrate, lipid and phosphorus components. The proteins were run on a 7.5% native PAGE. lane 1, marker; lane 2, plasma (diluted 20-fold) of fish injected with E2; lane 3, plasma (diluted 20-fold) of fish injected with 0.9% NaCl; lane 4, purified Vg; lanes 5, 6 and 7, purified Vg stained with Schiff reagent, methyl green and Sudan black B, respectively. The protein induced by E2 stained positive for carbohydrate, lipid, and phosphorus. (B) Peptide mass mapping of the purified protein.

Mentions: In fishes, Vg is a protein with a molecular weight ranging from 250 kDa to 600 kDa [28], [29]. Compared with untreated fish, plasma from 17-β-estradiol (E2)-injected H. otakii had an intense band of protein with a molecular mass of ∼450 kDa (Fig. 1A lanes 2 and 3), suggesting that it was E2-inducible protein. The protein from E2-injected fishes was purified by double-step chromatography (Fig. 1A lane 4), and the purified protein stained positive for carbohydrate, lipid, and phosphorus (Fig. 1A lanes 5, 6 and 7), thus establishing the protein as a phospholipoglycoprotein. Peptide mass mapping analysis performed on an Applied Biosystems 4700 proteomics analyzer further revealed that the protein purified was Vg from fish H. otakii (Fig. 1B).


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

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

Purification and identification of Vg.(A) Purification of Vg and determination of carbohydrate, lipid and phosphorus components. The proteins were run on a 7.5% native PAGE. lane 1, marker; lane 2, plasma (diluted 20-fold) of fish injected with E2; lane 3, plasma (diluted 20-fold) of fish injected with 0.9% NaCl; lane 4, purified Vg; lanes 5, 6 and 7, purified Vg stained with Schiff reagent, methyl green and Sudan black B, respectively. The protein induced by E2 stained positive for carbohydrate, lipid, and phosphorus. (B) Peptide mass mapping of the purified protein.
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Related In: Results  -  Collection

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getmorefigures.php?uid=PMC2277463&req=5

pone-0001940-g001: Purification and identification of Vg.(A) Purification of Vg and determination of carbohydrate, lipid and phosphorus components. The proteins were run on a 7.5% native PAGE. lane 1, marker; lane 2, plasma (diluted 20-fold) of fish injected with E2; lane 3, plasma (diluted 20-fold) of fish injected with 0.9% NaCl; lane 4, purified Vg; lanes 5, 6 and 7, purified Vg stained with Schiff reagent, methyl green and Sudan black B, respectively. The protein induced by E2 stained positive for carbohydrate, lipid, and phosphorus. (B) Peptide mass mapping of the purified protein.
Mentions: In fishes, Vg is a protein with a molecular weight ranging from 250 kDa to 600 kDa [28], [29]. Compared with untreated fish, plasma from 17-β-estradiol (E2)-injected H. otakii had an intense band of protein with a molecular mass of ∼450 kDa (Fig. 1A lanes 2 and 3), suggesting that it was E2-inducible protein. The protein from E2-injected fishes was purified by double-step chromatography (Fig. 1A lane 4), and the purified protein stained positive for carbohydrate, lipid, and phosphorus (Fig. 1A lanes 5, 6 and 7), thus establishing the protein as a phospholipoglycoprotein. Peptide mass mapping analysis performed on an Applied Biosystems 4700 proteomics analyzer further revealed that the protein purified was Vg from fish H. otakii (Fig. 1B).

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