Chemical Component and Proteomic Study of the Amphibalanus (= Balanus) amphitrite Shell

Zhang, Gen; He, Lisheng; Wong, Yue-Him; Xü, Ying; Qian, Pei‐Yuan

doi:10.1371/journal.pone.0133866

Cited by 20 publications

(22 citation statements)

References 53 publications

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“…These proteins are expressed specifically in the adhesive plaque; they were identified using mRNA sequences derived from sub-mantle tissues where cement glands and other cement proteins are found34. GSrCPs were not found in translated mRNA libraries assembled from other regions of the organism (main body, side plates48), or in MS/MS analysis of fluid collected from canals that line the side plates. Furthermore, both filtered and unfiltered searches against all arthropod nrNCBI sequences yield no homologies to known cuticle proteins, which are in intimate contact with the cement13.…”

Section: Discussionmentioning

confidence: 99%

Sequence basis of Barnacle Cement Nanostructure is Defined by Proteins with Silk Homology

Fears

Leary

et al. 2016

Sci Rep

194

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Barnacles adhere by producing a mixture of cement proteins (CPs) that organize into a permanently bonded layer displayed as nanoscale fibers. These cement proteins share no homology with any other marine adhesives, and a common sequence-basis that defines how nanostructures function as adhesives remains undiscovered. Here we demonstrate that a significant unidentified portion of acorn barnacle cement is comprised of low complexity proteins; they are organized into repetitive sequence blocks and found to maintain homology to silk motifs. Proteomic analysis of aggregate bands from PAGE gels reveal an abundance of Gly/Ala/Ser/Thr repeats exemplified by a prominent, previously unidentified, 43 kDa protein in the solubilized adhesive. Low complexity regions found throughout the cement proteome, as well as multiple lysyl oxidases and peroxidases, establish homology with silk-associated materials such as fibroin, silk gum sericin, and pyriform spidroins from spider silk. Distinct primary structures defined by homologous domains shed light on how barnacles use low complexity in nanofibers to enable adhesion, and serves as a starting point for unraveling the molecular architecture of a robust and unique class of adhesive nanostructures.

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Section: Discussionmentioning

confidence: 99%

Sequence basis of Barnacle Cement Nanostructure is Defined by Proteins with Silk Homology

Fears

Leary

et al. 2016

Sci Rep

194

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“…Matsubara et al (2008) isolated two C-type lectin proteins BRA-2 and BRA-3 from the regenerating M. rosa shell. Zhang et al (2015) reported a list of acid-soluble shell proteins, including carbonic anhydrase and an aspartic acid-rich partial protein sequence from the intertidal barnacle Amphibalanus amphitrite. The aspartic acid-rich partial protein, however, has shown no sequence homology to the molluscan Asprich shell protein family (Gotliv et al 2005), Fig.…”

Section: Introductionmentioning

confidence: 99%

Identification of Barnacle Shell Proteins by Transcriptome and Proteomic Approaches

et al. 2018

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In barnacle shell, the calcified shell layer is laid on top of the epicuticle. Here, we report our strategy and some preliminary results on the identification of potential shell proteins of the barnacle Megabalanus rosa. At first, M. rosa proteins from acid-soluble and acid-insoluble shell extracts were subjected to proteomic analysis and searched against M. rosa complete transcriptome. Then using the information that the calcified shell is formed just after the larval-adult molt, juvenile

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“…SIPC is highly expressed in barnacle shells 5 . It has been hypothesized that SIPC binds tightly to shell components (such as chitin or minerals), because a strong buffer (containing SDS and DTT) is required to extract SIPC from barnacle shells 16 . Moreover, inhibition of p38 MAPK pathway 17 and elevation of endogenous nitric oxide concentration 18 both decrease the expression level of SIPC in cyprids.…”

mentioning

confidence: 99%

Secretory locations of SIPC in Amphibalanus amphitrite cyprids and a novel function of SIPC in biomineralization

Zhang

Yang

Leung

et al. 2016

Sci Rep

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Settlement-inducing protein complex (SIPC) is a pheromone that triggers conspecific larval settlement in the barnacle Amphibalanus amphitrite. In the present study, immunostaining and scanning electron microscopy of SIPC revealed signals in the frontal horn pores and the secretions from carapace pores, suggesting that SIPC might be directly secreted from these organs in A. amphitrite cyprids. Further observations showed that the frontal horn pores could contact surfaces while cyprids were “walking”. Immunostaining for SIPC on the contacted surfaces displayed SIPC signals. These signals were similar to the frontal horn pores in size and morphology, suggesting that frontal horn pores might deposit SIPC. Besides, full-length SIPC was expressed and subsequent assays indicated that recombinant SIPC was able to bind to chitins and induce the precipitation of CaCO3. Furthermore, recombinant SIPC inhibited the formation of vaterites and regulated the morphology of calcite crystals. The crystals that formed with recombinant SIPC were more stable against water erosion. Overall, these results reported a novel function of recombinant SIPC that regulates crystal formation in barnacle shells.

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Chemical Component and Proteomic Study of the Amphibalanus (= Balanus) amphitrite Shell

Cited by 20 publications

References 53 publications

Sequence basis of Barnacle Cement Nanostructure is Defined by Proteins with Silk Homology

Sequence basis of Barnacle Cement Nanostructure is Defined by Proteins with Silk Homology

Identification of Barnacle Shell Proteins by Transcriptome and Proteomic Approaches

Secretory locations of SIPC in Amphibalanus amphitrite cyprids and a novel function of SIPC in biomineralization

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