Vitellogenin, a multivalent sensor and an antimicrobial effector

Zhang, Shicui; Wang, Shaohui; Li, Hongyan; Li, L i

doi:10.1016/j.biocel.2010.11.003

Cited by 130 publications

(93 citation statements)

References 28 publications

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“…This result was similar to the previous study of Vg in male zebra fish D. rerio (Tong et al 2010). In the innate immune system, Vgs have repeatedly been reported to act as multivalent PRR, a bactericidal molecule or an acute-phase protein (Zhang et al 2011a). As specific pathogen-associated molecular patterns (PAMPs), both LPS and LTA can be recognized by PRRs to initiate immune responses (Akira et al 2006, Kumar et al 2009).…”

Section: Immunoprotection Function Of Vtg2/vnsupporting

confidence: 80%

“…Vg in fish acts as a multivalent pattern recognition receptor (PRR), a bactericidal molecule or an acutephase protein in innate immunity. For instance, Vg has multiple specificities capable of identifying bacterium, virus and an antimicrobial effector, as well as causing damage to the microbes and enhancing phagocytosis (Zhang et al 2011a).…”

Section: Introductionmentioning

confidence: 99%

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Vitellogenin2: spermatozoon specificity and immunoprotection in mud crabs

Yang¹,

Zheng²,

Bao³

et al. 2016

Reproduction

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As the precursor of vitellin (Vn), vitellogenin (Vg) has initially been considered as a female-specific protein involved in vitellogenesis, while it was also present in males induced by hormones or organs manipulation. Distinct from vtg1 we previously found in female mud crab Scylla paramamosain, vtg2 was intriguingly detected in male testis under normal physiological conditions in this study. Sequence analysis showed that vtg2 and vtg1 were actually two isoforms of Vg caused by different types of alternative splicing. PCR and in situ hybridization analysis revealed that vtg2 was localized only in the testicular spermatozoa, while Vn was detected in both the spermatozoa of the testis and seminal vesicle. Therefore, we speculated that Vn was initially translated in testicular spermatozoa, then migrated with spermatozoa, and finally stored in the seminal vesicle, where spermatozoa gradually accomplished maturation. We presumed that vtg2/Vn might act as an immune-relevant molecule in the male reproduction system. In the subsequent experiment, the expression of vtg2/Vn in testis was significantly induced in response to lipopolysaccharide (LPS) and lipoteichoic acid (LTA) injection at both transcriptional and translational levels. In the light of the results presented above, we deemed that vtg2/Vn is a novel candidate of immune-relevant molecules involved in immunoprotection during the spermatozoon maturation, and this research helps to open a new avenue for further exploring the role of Vg.Reproduction (2016) 152 235-243

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Section: Immunoprotection Function Of Vtg2/vnsupporting

confidence: 80%

Section: Introductionmentioning

confidence: 99%

Vitellogenin2: spermatozoon specificity and immunoprotection in mud crabs

Yang¹,

Zheng²,

Bao³

et al. 2016

Reproduction

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“…Although Vtgs are best known as the major components of yolk, there is a growing awareness that Vtg-like lipoproteins can have functions outside the yolk, such as immune protection and spermegg recognition in vertebrates (Campanella et al, 2011;Zhang et al, 2011), and clotting and melanization in arthropod hemolymph (Hall et al, 1999;Lee et al, 2000). Cv-d demonstrates a new and important function in BMP signaling.…”

Section: Discussionmentioning

confidence: 99%

Crossveinless d is a vitellogenin-like lipoprotein that binds BMPs and HSPGs, and is required for normal BMP signaling in the Drosophila wing

et al. 2012

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SUMMARYThe sensitivity of the posterior crossvein in the pupal wing of Drosophila to reductions in the levels and range of BMP signaling has been used to isolate and characterize novel regulators of this pathway. We show here that crossveinless d (cv-d) mutations, which disrupt BMP signaling during the development of the posterior crossvein, mutate a lipoprotein that is similar to the vitellogenins that comprise the major constituents of yolk in animal embryos. Cv-d is made in the liver-like fat body and other tissues, and can diffuse into the pupal wing via the hemolymph. Cv-d binds to the BMPs Dpp and Gbb through its Vg domain, and to heparan sulfate proteoglycans, which are well-known for their role in BMP movement and accumulation in the wing. Cv-d acts over a long range in vivo, and does not have BMP co-receptor-like activity in vitro. We suggest that, instead, it affects the range of BMP movement in the pupal wing, probably as part of a lipid-BMP-lipoprotein complex, similar to the role proposed for the apolipophorin lipid transport proteins in Hedgehog and Wnt movement.

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“…This lipoprotein has a broad-range of antibacterial, antiviral, and antifungal effects as shown in several fish species [38][39][40][41] . Piscine vitellogenin gene expression is upregulated upon infection -the protein recognizes bacterial and fungal surface components, and facilitates phagocytosis of the pathogens [38] .…”

Section: Vitellogenin In Immunitymentioning

confidence: 99%

Vitellogenin in inflammation and immunity in social insects

2017

Inflamm Cell Signal

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Social insects, such as the honey bee and ants, form vast colonies that are only rivalled by human settlements. Living in dense, often stationary groups is prone to increase disease transmission. Yet, social insect queens and certain worker types can lead lengthy lives compared to the life span of most solitary insects. Social insects appear to have modified insulin/insulin like signaling pathway that regulates insect life history. This modification results in extremely elevated levels of the multifunctional lipoprotein vitellogenin in the individuals with longer life span. Vitellogenin is an egg-yolk precursor, but it also regulates caste-related behaviors in social insects, has shielding effects in inflammation and infection, and it is a mediator of transgenerational immunity. Here, we compile what is known about the life span and immune actions of vitellogenin and the evolution of this protein in the honey bee and ants. Recently we identified proteins homologous to vitellogenin in several Hymenopteran species, and showed that at least one of these vitellogenin-like proteins can have a protective role similar to vitellogenin in the honey bee. The newly identified vitellogenin homologs hint that the regulation of social insect life span can be more complex than thought before.

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Vitellogenin, a multivalent sensor and an antimicrobial effector

Cited by 130 publications

References 28 publications

Vitellogenin2: spermatozoon specificity and immunoprotection in mud crabs

Vitellogenin2: spermatozoon specificity and immunoprotection in mud crabs

Crossveinless d is a vitellogenin-like lipoprotein that binds BMPs and HSPGs, and is required for normal BMP signaling in the Drosophila wing

Vitellogenin in inflammation and immunity in social insects

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