Patterns of larval food production by hypopharyngeal glands in adult worker honey bees

Knecht, Damian; Kaatz, Hans-Hinrich

doi:10.1051/apido:19900507

Cited by 146 publications

(138 citation statements)

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“…The synthesis of royal jelly (RJ) takes place in HPGs; and ca. 82% of RJ proteins belong to the major royal jelly proteins (MRJP) (Knecht & Kaatz, 1990;Schmitzová et al, 1998). The above results confirm the presence of four major proteins of RJ (i.e., 50, 56, 57, and 64 kDa) (Hanes & Šimuth, 1992;Kubo et al, 1996).…”

Section: Discussionsupporting

confidence: 73%

The influence of sublethal doses of imidacloprid on protein content and proteolytic activity in honey bees (Apis mellifera L.)

Wilde

Frączek

Siuda

et al. 2016

Journal of Apicultural Research

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The effect of sublethal doses of imidacloprid on protein content and activity of proteases on honey bees was analyzed. The study was conducted in three experimental groups: colonies from groups BE-5 and BE-200 were contaminated with 5 and 200 ppb of imidacloprid, respectively, via their food supply (syrup and pollen), while group BE was used as control (untreated). Bee samples were collected 3 and 10 weeks after feeding started. Protein concentration in bee tissue extracts was analyzed with reference: (a) to the dose of imidacloprid; and (b) duration of exposure to the chemical. The average quantity of protein content was significantly higher at the 3-week interval than in the 10-week interval and the bees from control colonies (BE) had significantly higher protein contents than contaminated bees (BE-5 and BE-200), even 3 weeks after feeding with imidacloprid started. Similarly, the activity of proteolytic enzymes (proteases) was found to be dependent on the dose of imidacloprid used, compared to bees from control colonies showing significantly higher activity.Influencia de las dosis subletales de Imidacloprid en el contenido de proteína y la actividad proteolítica en las abejas melíferas (Apis mellifera L.)Se ha analizado el efecto de las dosis subletales de imidacloprid en el contenido de proteínas y la actividad de las proteasas en las abejas melíferas. El estudio se realizó en tres grupos experimentales: las colonias de los grupos de BE-5 y BE-200 se contaminaron con 5 y 200 ppb de imidacloprid, respectivamente, a través del alimento suministrado (jarabe y polen), mientras que el grupo SER se utilizó como control (sin tratar). Se recogieron muestras de abejas en las semanas 3 y 10 después del comienzo de la alimentació n. La concentració n de proteína en extractos de tejido de abejas se analizó en relació n con: a) la dosis de imidacloprid; y b) la duració n de la exposició n a la sustancia química. La cantidad promedio del contenido de proteína fue significativamente mayor en el intervalo de 3 semanas que en el intervalo de 10 semanas y las abejas de las colonias control (BE) tuvieron un contenido de proteína significativamente más alto que las abejas contaminadas (BE-5 y BE-200), incluso 3 semanas después de que comenzara la alimentació n con imidacloprid. Del mismo modo se encontró que la actividad de las enzimas proteolíticas (proteasas) depende de la dosis de imidacloprid usada, en comparació n con las abejas de colonias de control que muestran una actividad significativamente más alta.

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Section: Discussionsupporting

confidence: 73%

The influence of sublethal doses of imidacloprid on protein content and proteolytic activity in honey bees (Apis mellifera L.)

Wilde

Frączek

Siuda

et al. 2016

Journal of Apicultural Research

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“…The HPGs are specialized for jelly production in young workers. In this stage, the organs are responsible for a substantial fraction of net protein synthesis (26), and the increase in size of the HPG acini in nurses is caused by the accumulation of a secretion reservoir of jelly (27). Binding of vitellogenin to the HPG membrane ( Fig.…”

Section: Discussionmentioning

confidence: 99%

“…For example, in species exhibiting a temporal caste structure such as the ant Pogonomyrmex owyheei and the wasp Polybia occidentalis, workers are drained of nutritional reserves before they start foraging (28,31). In the case of honeybees, turning off vitellogenin synthesis in the forager (4) and reprogramming its HPGs to synthesise honey-processing enzymes at low rates (27) is probably a means to economize the colony's protein household, as this will prevent buildup of a vitellogenin store that will be lost when the forager perishes in the field (13). Moreover, this seems to have opened up for further specialization of the forager physiology.…”

Section: Discussionmentioning

confidence: 99%

Social exploitation of vitellogenin

Amdam¹,

Norberg²,

Hagen³

et al. 2003

Proc. Natl. Acad. Sci. U.S.A.

351

295

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Vitellogenin is a female-specific glucolipoprotein yolk precursor produced by all oviparous animals. Vitellogenin expression is under hormonal control, and the protein is generally synthesized directly before yolk deposition. In the honeybee (Apis mellifera), vitellogenin is not only synthesized by the reproductive queen, but also by the functionally sterile workers. In summer, the worker population consists of a hive bee group performing a multitude of tasks including nursing inside the nest, and a forager group specialized in collecting nectar, pollen, water, and propolis. Vitellogenin is synthesized in large quantities by hive bees. When hive bees develop into foragers, their juvenile hormone titers increase, and this causes cessation of their vitellogenin production. This inverse relationship between vitellogenin synthesis and juvenile hormone is opposite to the norm in insects, and the underlying proximate processes and life-history reasons are still not understood. Here we document an alternative use of vitellogenin by showing that it is a source for the proteinaceous royal jelly that is produced by the hive bees. Hive bees use the jelly to feed larvae, queen, workers, and drones. This finding suggests that the evolution of a brood-rearing worker class and a specialized forager class in an advanced eusocial insect society has been directed by an alternative utilization of yolk protein.

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“…Caste determination in honey-bees is due by larval diet rather than by a genetic predisposition of some of them to become queens or workers [3]. Nurse bees produce royal jelly (RJ) in their glandular cephalic system (hypopharingeal and mandibular glands) between the sixth and twelfth day of their image life [6][7][8]. All the larvae within three days after hatching are fed with RJ by nurse bees; after the first three days of larval development the queen-designate larvae continue to be fed with RJ throughout development, while those designated to be workers undergo a diet made up of a mixture of the nurse bees mandibular secretion, honey and pollen (worker jelly) [9][10][11][12].…”

Section: Introductionmentioning

confidence: 99%

Towards royal jelly proteome

et al. 2005

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The recent availability of the honey-bee Apis mellifera genome and trascriptome of both the female castes, has stimulated new efforts in investigating the protein composition of royal jelly (RJ), its role in caste differentiation and its quality and typicality by a proteomic approach. This study is aimed both to separate and identify proteins of royal jelly and to detect some of them in honey-bee pollen-bread by using two-dimensional gel electrophoresis, mass spectrometry and by de novo sequencing. All the identified proteins belonged to the Apis mellifera genome. Apalbumin 1 was also confirmed to be present in honey-bee pollen-bread where the presence of apalbumin 2 was also found. In addition several fragments of apalbumin 1 and apalbumin 3 were also found in RJ. These could be the result of protease activity other than that of serine-protease. This study is a contribution to the description of royal jelly proteome.

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Patterns of larval food production by hypopharyngeal glands in adult worker honey bees

Cited by 146 publications

References 0 publications

The influence of sublethal doses of imidacloprid on protein content and proteolytic activity in honey bees (Apis mellifera L.)

The influence of sublethal doses of imidacloprid on protein content and proteolytic activity in honey bees (Apis mellifera L.)

Social exploitation of vitellogenin

Towards royal jelly proteome

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