Molecular characterization of iron binding proteins, transferrin and ferritin heavy chain subunit, from the bumblebee Bombus ignitus

Wang, Dong; Kim, Bo Yeon; Lee, Kwang-Sik; Yoon, Hyung Joo; Zheng, Chengchao; Lü, Wei; Jia, Jing; Kim, Doh Hoon; Sohn, Hung Dae; Jin, Byung Rae

doi:10.1016/j.cbpb.2008.09.082

Cited by 46 publications

(41 citation statements)

References 51 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…With regards to the N-lobe, a change of His to Glu at residue 249 is found in Tsf1 from several insects including, B. ignitus, R. clavatus, C. fumiferana, B. mori, P. xylostella, M. sexta, A. aegypti, A. germari, P. brevitarsis, M. darwiniensis and B. discoidalis (Table 3). This change preserves iron binding and allows a faster rate of iron release [13,30,31,[41][42][43]81,83,88,99] suggesting conditions of iron release in some insects could differ from those of mammals. Although the flies, Sarcophaga, Drosophila and Glossina, also have an Asp to Glu change in the N-lobe binding site, the iron binding in this lobe is conserved (Table 3; [30,33,36,45,74,75]).…”

Section: Sequencementioning

confidence: 96%

“…Both sequences show high identity to MsTsf1 (Table 2) and have predicted glycosylation sites [81], as does Tsf1 from Chilo suppressalis (CsTsf1; Lepidoptera; striped riceborer; [82]). Further, Tsf1 from the Hymenopterans, Bombus ignitus (BiTsf1; bumble bee; [83]) and Apis mellifera (AmTsf1; honey bee; [46,84,85]) is predicted from sequence analysis to be~75 kDa (Table 1a). The molecular weight of BiTsf1 was confirmed by Western blotting as~79 kDa and sequence analysis identified several putative glycosylation sites.…”

Section: Features Of Genomic and Primary Structurementioning

confidence: 99%

See 1 more Smart Citation

Insect transferrins: Multifunctional proteins

Geiser

Winzerling

2012

Biochimica et Biophysica Acta (BBA) - General Subjects

115

View full text Add to dashboard Cite

Section: Sequencementioning

confidence: 96%

Section: Features Of Genomic and Primary Structurementioning

confidence: 99%

Insect transferrins: Multifunctional proteins

Geiser

Winzerling

2012

Biochimica et Biophysica Acta (BBA) - General Subjects

115

View full text Add to dashboard Cite

“…Mammals have a relatively low concentration of extracellular ferritin in the serum and synovial and cerebrospinal fluids, which has been implicated as an inflammatory indicator and possibly a component of immune response (MeyronHoltz et al, 2011;Orino and Watanabe, 2008). In insects and other invertebrates, ferritin has been implicated in response to bacterial infections (Kremer et al, 2009;Wang et al, 2009;Zheng et al, 2010). The blood meal of ticks may also expose them to various pathogens.…”

Section: Table1 Effects Of Hlfer1 and Hlfer2 Silencing On Blood Feementioning

confidence: 99%

Multiple ferritins are vital to successful blood feeding and reproduction of the hard tick Haemaphysalis longicornis

Galay

Aung

Umemiya‐Shirafuji

et al. 2013

Journal of Experimental Biology

View full text Add to dashboard Cite

SUMMARYTicks are obligate hematophagous parasites and important vectors of diseases. The large amount of blood they consume contains great quantities of iron, an essential but also toxic element. The function of ferritin, an iron storage protein, and iron metabolism in ticks need to be further elucidated. Here, we investigated the function a newly identified secreted ferritin from the hard tick Haemaphysalis longicornis (HlFER2), together with the previously identified intracellular ferritin (HlFER1). Recombinant ferritins, expressed in Escherichia coli, were used for anti-serum preparation and were also assayed for iron-binding activity. RT-PCR and western blot analyses of different organs and developmental stages of the tick during blood feeding were performed. The localization of ferritins in different organs was demonstrated through an indirect immunofluorescent antibody test. RNA interference (RNAi) was performed to evaluate the importance of ferritin in blood feeding and reproduction of ticks. The midgut was also examined after RNAi using light and transmission electron microscopy. RT-PCR showed differences in gene expression in some organs and developmental stages. Interestingly, only HlFER2 was detected in the ovary during oviposition and in the egg despite the low mRNA transcript. RNAi induced a reduction in post-blood meal body weight, high mortality and decreased fecundity. The expression of vitellogenin genes was affected by silencing of ferritin. Abnormalities in digestive cells, including disrupted microvilli, and alteration of digestive activity were also observed. Taken altogether, our results show that the iron storage and protective functions of ferritin are crucial to successful blood feeding and reproduction of H. longicornis. Supplementary material available online at

show abstract

“…The presence of isoferritins in different tissues had been attributed to post-translational modifications such as deamidation, deacylation, and glycosylation (Harrison and Arosio 1996). Gene expression and proteomic studies have indicated that bacterial infection or LPS challenge can lead to up-regulation of the Drosophila and bumblebee FerH (Levy et al 2004;Vierstraete et al 2004;Wang D. et al 2009). Genomewide expression studies in Drosophila melanogaster have also established that ferritin genes are up-regulated in response to oxidative stress, suggesting an antioxidant role (Zou et al 2000;Landis et al 2004).…”

Section: Discussionmentioning

confidence: 97%

“…Genomewide expression studies in Drosophila melanogaster have also established that ferritin genes are up-regulated in response to oxidative stress, suggesting an antioxidant role (Zou et al 2000;Landis et al 2004). Moreover, the expression profile of ferritin is acutely induced in the fat body of Bombus ignitus worker bees in response to stressors such as wounding, bacterial challenge, and iron overload (Wang D. et al 2009). …”

Section: Discussionmentioning

confidence: 98%

Isolation and Gene Expression of Yellow Grouper Ferritin Heavy Chain Subunit After Lipopolysaccharide Treatment

Wang

Wei

2012

Biochem Genet

View full text Add to dashboard Cite

Ferritin is a ubiquitous and conserved iron storage protein that plays a central role in iron metabolism. The ferritin heavy chain subunit (FerH) homolog was isolated from yellow grouper (Epinephelus awoara) spleen using suppression subtractive hybridization and RACE-PCR. The nucleotide sequence of FerH full-length cDNA was 1173 bp and contained an open reading frame of 534 bp, encoding a putative protein of 177 amino acids. The encoded protein shows 78-94% identity with homologs. Based on phylogenetic analysis, yellow grouper FerH is highly conserved throughout evolution and is closer to European seabass than to other species. RT-PCR analysis demonstrated that FerH was widely expressed in various healthy tissues and significantly up-regulated in liver, spleen, and anterior kidney by lipopolysaccharide. The results suggest that yellow grouper FerH may play a role in immune response.

show abstract

Molecular characterization of iron binding proteins, transferrin and ferritin heavy chain subunit, from the bumblebee Bombus ignitus

Cited by 46 publications

References 51 publications

Insect transferrins: Multifunctional proteins

Insect transferrins: Multifunctional proteins

Multiple ferritins are vital to successful blood feeding and reproduction of the hard tick Haemaphysalis longicornis

Isolation and Gene Expression of Yellow Grouper Ferritin Heavy Chain Subunit After Lipopolysaccharide Treatment

Contact Info

Product

Resources

About