Vitellogenin (VTG or less popularly known as VG) (from Latin vitellus, yolk, and genero, I produce) is a precursor of egg yolk that transports protein and some lipid from the liver through the blood to the growing oocytes where it becomes part of the yolk. Normally, it is only found in the blood or hemolymph of females, and can therefore be used as a biomarker in vertebrates of exposure to environmental estrogens which stimulate elevated levels in males as well as females.[1] "Vitellogenin" is a synonymous term for the gene and the expressed protein. The protein product is classified as a glycolipoprotein, having properties of a sugar, fat and protein. It belongs to a family of several lipid transport proteins.

Vitellinogen, open beta-sheet
Available protein structures:
Pfam  structures / ECOD  
PDBsumstructure summary

Vitellogenin is an egg yolk precursor found in the females of nearly all oviparous species including fish, amphibians, reptiles, birds, most invertebrates, and monotremes.[2] Vitellogenin is the precursor of the lipoproteins and phosphoproteins that make up most of the protein content of yolk. In the presence of estrogenic endocrine disruptive chemicals (EDCs), male fish can express the gene in a dose dependent manner. This gene expression in male fish can be used as a molecular marker of exposure to estrogenic EDCs.[3]



Vitellogenin provides the major egg yolk protein that is a source of nutrients during early development of egg-laying (oviparous) vertebrates and invertebrates. Although vitellogenin also carries some lipid for deposition in the yolk, the primary mechanism for deposition of yolk lipid is instead via VLDLs, at least in birds and reptiles.[4] Vitellogenin precursors are multi-domain apolipoproteins (proteins that bind to lipids to form lipoproteins), that are cleaved into distinct yolk proteins. Different vitellogenin proteins exist, which are composed of variable combinations of yolk protein components; however, the cleavage sites are conserved.[citation needed]



In vertebrates, a complete vitellogenin is composed of:

N-terminal lipid transport domain

Vitellogenin lipid transport domain, N-terminal
OPM superfamily254
OPM protein1lsh
Available protein structures:
Pfam  structures / ECOD  
PDBsumstructure summary

This particular domain represents a conserved region found in several lipid transport proteins, including vitellogenin, microsomal triglyceride transfer protein and apolipoprotein B-100.[7]

Vesicle trafficking


This particular domain, the Vitellogenin lipid transport domain, is also found in the Microsomal triglyceride transfer protein (MTTP) and in Apolipoprotein B. It aids cell trafficking and export of cargo.[citation needed]

Microsomal triglyceride transfer protein (MTTP)


Microsomal triglyceride transfer protein (MTTP) is an endoplasmic reticulum lipid transfer protein involved in the biosynthesis and lipid loading of apolipoprotein B. MTTP is also involved in the late stage of CD1d trafficking in the lysosomal compartment, CD1d being the MHC I-like lipid antigen presenting molecule.[8]

Apolipoprotein B


Apolipoprotein B can exist in two forms: B-100 and B-48. Apolipoprotein B-100 is present on several lipoproteins, including very low-density lipoproteins (VLDL), intermediate density lipoproteins (IDL) and low density lipoproteins (LDL), and can assemble VLDL particles in the liver.[9] Apolipoprotein B-100 has been linked to the development of atherosclerosis.

ApoB is ancestrally universal to all animals, as homologs are found in choanoflagellates. The insect homolog is called apolipophorin I/II.[10]

Human proteins containing this domain


APOB (see native LDL-ApoB structure at 37°C on YouTube);[11] MTTP;

Honey bees


Honey bees deposit vitellogenin molecules in fat bodies in their abdomen and heads. The fat bodies apparently act as a food storage reservoir. The glycolipoprotein vitellogenin has additional functionality as it acts as an antioxidant to prolong Queen bee and forager lifespan as well as a hormone that affects future foraging behavior.[12] The health of a honey bee colony is dependent upon the vitellogenin reserves of the nurse bees – the foragers having low levels of vitellogenin. As expendable laborers, the foragers are fed just enough protein to keep them working their risky task of collecting nectar and pollen. Vitellogenin levels are important during the nest stage and thus influence honey bee worker division of labor.[citation needed]

A nurse bee's vitellogenin titer that developed in the first four days after emergence, affects its subsequent age to begin foraging and whether it preferentially forages for nectar or pollen. If young workers are short on food their first days of life, they tend to begin foraging early and preferentially for nectar. If they are moderately fed, they forage at normal age preferentially for nectar. If they are abundantly fed, immediately after emergence, their vitellogenin titer is high and they begin foraging later in life, preferentially collecting pollen. Pollen is the only available protein source for honey bees.[13]

Juvenile hormone feedback loop


For the majority of the investigated insect species it has been documented that juvenile hormone stimulates the transcription of the vitellogenin genes and the consequent control of vitellogenin production (cf. Engelmann, 1983; Wyatt and Davey, 1996).[14][15]

The vitellogenin expression is part of a regulatory feedback loop that enables vitellogenin and juvenile hormone to mutually suppress each other. Vitellogenin and juvenile hormone likely work antagonistically in the honey bee to regulate the honey bees development and behavior. Suppression of one leads to high titers of the other.[16]

It is likely that the balance between vitellogenin and juvenile hormone levels is also involved in swarming behavior.[17]

Juvenile hormone levels drop in honey bee colonies pre-swarming and it is expected that vitellogenin levels would therefore rise. One may surmise, that swarming bees would want to pack along as much vitellogenin as possible to extend their lifespan and to be able to quickly build a new nest. [citation needed]



Vertebrates started off with a single copy of the vitellogenin gene, and the bird-mammalian and amphilian lineages each experienced duplications that gave rise to the modern genes. With the exception of monotremes, mammals have all their vitellogenin genes turned into pseudogenes, although the region syntenic to bird VIT1-VIT2-VIT3 can still be found and aligned.[18] In monotremes just one of the genes remained functional.[19]

See also



  1. ^ "Definition of VITELLOGENIN".
  2. ^ Robinson, Richard (18 March 2008). "For Mammals, Loss of Yolk and Gain of Milk Went Hand in Hand". PLOS Biology. 6 (3): e77. doi:10.1371/journal.pbio.0060077. PMC 2267822. PMID 20076706.
  3. ^ Tran, Thi Kim Anh; Yu, Richard Man Kit; Islam, Rafiquel; Nguyen, Thi Hong Tham; Bui, Thi Lien Ha; Kong, Richard Yuen Chong; O'Connor, Wayne A.; Leusch, Frederic D.L.; Andrew-Priestley, Megan; MacFarlane, Geoff R. (May 2019). "The utility of vitellogenin as a biomarker of estrogenic endocrine disrupting chemicals in molluscs". Environmental Pollution. 248: 1067–1078. doi:10.1016/j.envpol.2019.02.056. hdl:10072/386355. PMID 31091639. S2CID 92464394.
  4. ^ Price, E. R. (2017). "The physiology of lipid storage and use in reptiles". Biological Reviews. 92 (3): 1406–1426. doi:10.1111/brv.12288. PMID 27348513. S2CID 7570705.
  5. ^ Finn, Roderick Nigel (1 June 2007). "Vertebrate Yolk Complexes and the Functional Implications of Phosvitins and Other Subdomains in Vitellogenins1". Biology of Reproduction. 76 (6): 926–35. doi:10.1095/biolreprod.106.059766. PMID 17314313.
  6. ^ Thompson, James R.; Banaszak, Leonard J. (July 2002). "Lipid−Protein Interactions in Lipovitellin". Biochemistry. 41 (30): 9398–409. doi:10.1021/bi025674w. PMID 12135361.
  7. ^ Anderson TA, Levitt DG, Banaszak LJ (July 1998). "The structural basis of lipid interactions in lipovitellin, a soluble lipoprotein". Structure. 6 (7): 895–909. doi:10.1016/S0969-2126(98)00091-4. PMID 9687371.
  8. ^ Sagiv, Yuval; Bai, Li; Wei, Datsen G.; Agami, Reuven; Savage, Paul B.; Teyton, Luc; Bendelac, Albert (16 April 2007). "A distal effect of microsomal triglyceride transfer protein deficiency on the lysosomal recycling of CD1d". The Journal of Experimental Medicine. 204 (4): 921–8. doi:10.1084/jem.20061568. PMC 2118556. PMID 17403933.
  9. ^ Olofsson SO, Borèn J (November 2005). "Apolipoprotein B: a clinically important apolipoprotein which assembles atherogenic lipoproteins and promotes the development of atherosclerosis". Journal of Internal Medicine. 258 (5): 395–410. doi:10.1111/j.1365-2796.2005.01556.x. PMID 16238675. S2CID 19885776.
  10. ^ Huebbe P, Rimbach G (August 2017). "Evolution of human apolipoprotein E (APOE) isoforms: Gene structure, protein function and interaction with dietary factors". Ageing Research Reviews. 37: 146–161. doi:10.1016/j.arr.2017.06.002. PMID 28647612. S2CID 3758905.
  11. ^ Kumar V, Butcher SJ, Öörni K, Engelhardt P, Heikkonen J, et al. (2011) Three-Dimensional cryoEM Reconstruction of Native LDL Particles to 16Å Resolution at Physiological Body Temperature. [1]
  12. ^ Oliver, Randy (August 2007). "Fat Bees Part 1". American Bee Journal.[verification needed]
  13. ^ Randy, Oliver (Aug 2007). "Fat Bees - Part 1". American Bee Journal: 714.
  14. ^ Engelmann F (1983). "Vitellogenesis controlled by juvenile hormone". In Downer RG, Laufer H (eds.). Endocrinology of Insects. New York: Alan R. Liss. pp. 259–270.
  15. ^ Wyatt GR, Davey KG (1996). "Cellular and Molecular Actions of Juvenile Hormone. II. Roles of Juvenile Hormone in Adult Insects". Advances in Insect Physiology Volume 26. Vol. 26. pp. 1–155. doi:10.1016/S0065-2806(08)60030-2. ISBN 9780120242269.
  16. ^ Hrassnigg, Norbert; Crailsheim, Karl (2005). "Differences in drone and worker physiology in honeybees (Apis mellifera)" (PDF). Apidologie. 36 (2): 255–277. doi:10.1051/apido:2005015.
  17. ^ Zeng, Zhijiang; Huang, Zachary Y.; Qin, Yuchuan; Pang, Huizhong (1 April 2005). "Hemolymph Juvenile Hormone Titers in Worker Honey Bees under Normal and Preswarming Conditions". Journal of Economic Entomology. 98 (2): 274–278. doi:10.1603/0022-0493-98.2.274. PMID 15889713. S2CID 198130721.
  18. ^ Brawand, David; Wahli, Walter; Kaessmann, Henrik; Phillippe, Hervé (18 March 2008). "Loss of Egg Yolk Genes in Mammals and the Origin of Lactation and Placentation". PLOS Biology. 6 (3): e63. doi:10.1371/journal.pbio.0060063. PMC 2267819. PMID 18351802.
  19. ^ Yang Zhou, Linda Shearwin-Whyatt, Guojie Zhang et al.: Platypus and echidna genomes reveal mammalian biology and evolution. In: Nature. 6 January 2021. doi:10.1038/s41586-020-03039-0. See also:

Further reading

This article incorporates text from the public domain Pfam and InterPro: IPR001747