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At least 109 records · Page 6Linked to original sources
PubMed2006

Mussel colonization of a high flow artificial benthic habitat: byssogenesis holds the key.

Water flow is an important characteristic determining the settlement and growth of macro-invertebrates in the marine environment. Intake systems of coastal power stations offer a unique opportunity to study the effect of water flow on benthic organisms under field conditions. The cooling water intake system of a tropical coastal power station is used as an experimental facility to study the effect of flow on the recruitment and growth of three mussel species, viz, Brachidontes variabilis, B. striatulus, and Modiolus philippinarum. The study was prompted by earlier observation that these mussels were numerically abundant in the biofouling community present inside the seawater intake tunnel of the power station, even though their occurrence in the benthic community in the coastal waters outside was only nominal. Recruitment data showed that the three mussel species very successfully colonised surfaces exposed to the intake mouth (characterised by relatively high flow) of the power station. Significant difference was observed in the recruitment recorded at the intake point and the ambient environment outside. Under high flow condition, the growth rates of all the three mussel species were uniformly enhanced. It is argued that recruitment of the different species is related to the number of byssus threads produced by each mussel and the strength of the byssus threads. The results indicate that byssus number and byssus strength of the mussels are important criteria that decide successful colonization and establishment in high flow environments.

Adaptation, Physiological↗
PubMed2006

Unidentified extracellular prokaryotes within the byssal threads of the deep-sea vent mussel Bathymodiolus azoricus.

Bacterial symbiosis and/or parasitism is widespread in hydrothermal bivalves, and is typically developed in gills, with a lower incidence in mantle and digestive glands, while it has never been described in byssus. Using ultrastructural examination, we provide evidence for the existence of a potentially new group of filamentous prokaryotic organism in Bathymodiolus azoricus byssus, with putative parasitic influence. Additionally, a cystic, undefined organism was found with an unclear physiological role within the spongy net of the byssus plaque. Our results indicate that in spite of its antibacterial protective sheath, byssus gives access to prokaryotic organisms becoming prone to failure through damaged collagen fibres.

Animals↗
PubMed2026

Identification and characterization of a wet adhesive protein extracted from Dreissena bugensis, the freshwater quagga mussel.

Mechanisms of wet adhesion have evolved in several aquatic organisms over millions of years. Yet, the repertoire of synthetic biocompatible wet adhesive materials is still limited. The byssus is a well-studied proteinaceous bioadhesive structure utilized by several bivalves to support sessile lifestyles in turbulent conditions. The quagga mussel (Dreissena bugensis) is a freshwater byssate and a notorious invasive species in the Great Lakes region. To identify adhesive proteins in the quagga mussel byssus, we utilized quantitative proteomics and found several proteins enriched at the byssus-substrate interface. Among the identified proteins was the Dbfp7 protein family. Dbfp7 is a small, polymorphic, and mostly disordered protein that lacks significant amounts of 3,4-dihydroxyphenylalanine (DOPA), a modified amino acid found in several marine mussel byssal proteins. Atomic force microscopy nanomechanical mapping of Dbfp7 films demonstrates that this protein exhibits adhesive ability in aqueous conditions. While DOPA is critical for marine mussel adhesion, interfacial electrochemistry of freshwater adhesive plaques suggests that freshwater byssates circumvent catechol-based adhesion. The functional characterization of Dbfp7 as a freshwater mussel adhesive protein advances the understanding of fundamental requirements for biocompatible wet adhesion, a crucial step for the development of bioinspired wet adhesive materials, such as improved medical adhesives.

Animals↗
PubMed2005

Byssal detachment underestimates tolerance of mussels to toxic compounds.

Mussels are sedentary organisms attached to solid substrata by means of byssus threads. Mussels detached from their substratum tend to reattach by producing new byssus threads. Therefore, in bioassays using mussels, if the test animals are in an unattached status, increased byssogenic activity would expose their soft body parts to the toxic compound used. We test the tolerance of two mussel species (Mytilopsis leucophaeata and Mytilus edulis) to an oxidizing biocide (chlorine) and show that detached mussels are 24-28% less tolerant than byssally attached ones. Detached mussels also showed higher oxygen consumption, filtration rate, foot activity, byssus thread production and byssogenesis index, parameters which are associated with valve opening. A review of literature showed that most of the published data on toxicity against heavy metals and biocides are generated using unattached mussels. The data, therefore, represent an underestimation of the toxicity of the tested compound. Correction data are presented for chlorine tolerance of Dreissena polymorpha, Mytilopsis leucophaeata and Mytilus edulis. The present study suggests the importance of maintaining mussels in their attached status, while undertaking toxicity bioassays.

Analysis of Variance↗
PubMed1981

Ultrastructural and cytochemical study on the enzyme gland of the foot of a mollusc.

The enzyme gland of the foot of the mussel Mytilus has been so far considered a gland producing and exporting a phenol oxidase catalysing the general tanning processes of byssus threads. In contrast, the present study shows that this gland produces mainly secretory granules which form the cortical layers of byssus threads. Cytochemical methods at the ultrastructural level (phosphotungstic acid at low pH, silver methenamine, periodic acid-thiosemicarbazide-silver proteinate, silver methenamine for sulphur-rich proteins demonstration) and enzyme digestion tests (pepsin, trypsin, alpha-chymotrypsin) indicate that secretory granules contain glycoproteins rich in sulphydryl groups and in aromatic amino acids. The cytochemical demonstration of phenol oxidase shows that enzyme activity is present in Golgi complex, whereas it is absent in secretory granules. For this reason, phenol oxidase does not seem to be exported and utilized for tanning of byssus threads, but it might rather be involved in the elaboration and tanning of the content of the secretory granules in the enzyme gland itself.

Amino Acids↗
PubMed1982

Photoaffinity labelling of dopamine receptors in molluscan smooth muscle.

Relaxation of catch contraction of the anterior byssus retractor muscle of the sea mussel Mytilus edulis L. by dopamine is mediated through a dopamine receptor but not through adrenoceptors (Takayanagi et al 1981). Photoaffinity labelling is a technique widely used in biochemical in vitro studies to test an interaction between a ligand and its binding site. Therefore, we tried photoaffinity labelling of the dopamine receptor in order to study the dopamine receptor in the anterior byssus retractor muscle of M. edulis. Sea mussels, collected from the east coast of Tokyo Bay were stored in aerated seawater (NaCl 456, KCl 11, CaCl2 2H2O 11, MgCl2 6H2O 48 nM and Tris-HCl 25 mM; pH 7 . 8 to 8 . 0) at 10 degrees C and used within a week of collection. Muscle bundles (about 1 mm in diameter) were dissected from the anterior byssus retractor muscle and suspended in a 10 ml organ bath filled with artificial seawater bubbled with air and kept at 24 to 25 degrees C. Responses to drugs were recorded isotonically under a tension of 0 . 2 g. After the muscle had been exposed to acetylcholine (10(-4)M) for 2 min to induce catch contraction and washed with artificial seawater for 5 min, dopamine was applied. Relaxations following a 10 min exposure to various doses of dopamine were estimated. The response to 3 x 10(-7) M dopamine was considered as the maximum response to obtain dose-response curves (Takayanagi et al 1981). To irradiate the muscle, a Toshiba lamp FL-20E (wavelength: 270 to 350 nm) was used as a light source. The muscle, immersed in artificial seawater containing dopamine (10(-4)M), was irradiated (1 cm from the lamp) for 25 min and then washed with artificial seawater for 60 min (Takayanagi et al 1976). After the muscle was irradiated in the presence of dopamine (10(-4)M) for 25 min and washed for 60 min, the dose-response curve of dopamine was shifted in a parallel way towards doses about 8 times higher (Fig. 1). This inhibition of dopamine-induced responses continued for at least 2 h. The dose-response curve for dopamine was unaffected when the muscle was incubated with both dopamine (10(-4)M) and haloperidol (10(-4)M) for 25 min under the irradiation conditions (Fig. 1). However, the inhibitory action of dopamine was unaffected when the muscle was irradiated in the absence of dopamine and washed for 60 min, suggesting that 20 min irradiation did not influence mechanisms for relaxation of this smooth muscle by dopamine. Furthermore, when the muscle was incubated with dopamine (10(-4)M) or haloperidol (10(-4)M) for 25 min and washed with artificial sea water, the dose-response curve for dopamine was not influenced. When promethazine (10(-4)M), an antihistamine drug found to have no antidopaminergic action in this muscle (Yoshida et al 1981), was used instead of haloperidol (10(-4)M), the dose response curve for dopamine was shifted after irradiation (data not shown). These results indicate the possibility that dopamine is photolysed to a reactive compound which reacts irreversibly with the dopamine receptor.

Affinity Labels↗
PubMed1986

Mussel glue from Mytilus californianus Conrad: a comparative study.

Marine mussels secrete a byssus in order to attach to solid surfaces in the sea. The polyphenolic protein is the "glue" in the adhesive plaques of the byssus. In Mytilus californianus, the polyphenolic protein has an apparent molecular weight of 85,000 +/- 5,000 and is rich in the amino acids lysine, 3,4-dihydroxyphenylalanine, serine, threonine, and hydroxyproline. In composition it resembles the polyphenolic protein of M. edulis (Mr = 125,000), although the M. edulis protein contains significantly less isoleucine and more alanine. Tryptic digestion of M. californianus polyphenolic protein revealed two types of repeating decapeptides (1) (Ser/Thr)-Thr-(Tyr/Dopa)-Hyp-Hyp-Thr-Dopa-Lys-Hyp-Lys and (2) Ile-(Thr/Ser)-(Tyr/Dopa)-Hyp-Hyp-Thr-Dopa-Lys-Hyp-Lys. Residues 2 to 8 are identical with residues 4-10 in M. edulis decapeptides.

Amino Acids↗
PubMed2006

Control of modiolid mussels in cooling water systems by continuous chlorination.

Modiolid mussels such as Modiolus philippinarum and Modiolus metcalfei constitute a numerically significant group in fouling communities, especially in tropical and subtropical industrial cooling water systems. Nevertheless, there are hardly any published reports on the tolerance of these species to chlorination or biofouling control measures, This article provides data on the mortality pattern (LT(50) and LT(100)) and physiological activities (oxygen consumption, filtration rate, foot activity, and byssus thread production) of different size groups of M. philippinarum (7- to 30-mm shell lengths) and M. metcalfei (6- to 26-mm shell lengths) exposed to different concentrations of residual chlorine (0.25, 0.50, 0.75, and 1.00 mg/L for sublethal responses; 1, 2, 3, and 5 mg/L for mortality). It is shown that exposure time for 100% mortality of M. philippinarum and M. metcalfei significantly decreased with increasing residual chlorine concentration. For example, 30-mm size group M. philippinarum exposed to 1 mg/L chlorine residual took 402 h to reach 100% mortality, whereas those exposed to 5 mg/L chlorine took 108 h. Among the two mussels, M. philippinarum showed slightly higher tolerance (9-20%) to chlorine when compared to M. metcalfei. The effect of mussel size on mortality of M. philippinarum was significant, with the larger size group mussels showing greater resistance than smaller ones. However, in M. metcalfei, size of the mussel does not seem to be a determinant of its chlorine tolerance. All size groups of M. philippinarum and M. metcalfei showed progressive reduction in physiological activities (oxygen consumption, filtration rate, foot activity index, and byssus thread production) when chlorine residuals gradually increased from 0 to 1 mg/L. Reduction in physiological activities was strongly correlated with chlorine concentration. A comparison of present data with data available for other coexisting mussel species suggests that M. philippinarum and M. metcalfei are relatively less tolerant to chlorine than Perna viridis, Perna perna, and Brachidontes striatulus, which also cause fouling problems in tropical coastal waters.

Animals↗
PubMed2000

Improved Plate Assay for Antifouling Substances Using Blue Mussel Mytilus edulis galloprovincialis.

An improved plate assay for screening antifoulants against blue mussels, Mytilus edulis galloprovincialis, was designed based on an assay contrived by Ina and colleagues. To obtain more reliable results, the number of test mussels for one sample was increased from 4 to 10. Cardboard pieces used as test plates were cut into rectangular shapes to separate the test sample and the blank zone, which are of the same area. Activity was expressed numerically. In this improved method, several inhibitors of byssus thread formation were isolated by using a smaller amount of sample per area than in the original method. Previously our laboratory developed a foot-stimulating bioassay for the same purpose. This method requires only a small amount of sample and is therefore useful for isolating antifouling substances from natural sources, including marine organisms. However, the inhibition of byssus thread formation cannot be directly evaluated in the foot-stimulating method. The improved plate assay and the foot-stimulating method were examined and compared using a secosterol from the sponge Dysidea granulosa and CuSO(4).

Journal Article↗
PubMed1987

Catch-relaxing peptide isolated from Mytilus pedal ganglia.

A peptide that relaxes catch tension of the anterior byssus retractor muscle of Mytilus edulis was purified from pedal ganglion extracts of the mussel. Its primary structure was determined to be H-Ala-Met-Pro-Met-Leu-Arg-Leu-NH2. This peptide was found to have not only catch-relaxing action on the byssus retractor muscle but also modulatory actions on contractions in various molluscan muscles.

Animals↗
PubMed2026

Transcriptomic analysis reveals the molecular mechanisms underlying the inhibition of Mytilus edulis attachment by biofouling control agents.

This study combined acute toxicity assays, phenotypic quantification, and transcriptomic profiling to systematically investigate the inhibitory effects and molecular regulatory mechanisms of a novel alkylamine-based antifouling agent on survival, byssus secretion, and attachment behavior of juvenile Mytilus edulis. The 96 h-LC50 of the agent to juvenile M. edulis was 8.84 mg/L, and 10 mg/L of the agent completely inhibited mussel attachment within 24 h, significantly reducing byssal thread number, length, and diameter while increasing detachment frequency, resulting in irreversible attachment failure. Transcriptomic analysis identified 2746 differentially expressed genes, which were mainly enriched in pathways including signal transduction, immune defense, stress response, cytoskeleton organization, and protein binding. KEGG and GSEA enrichment revealed that the antifouling agent activated the MAPK stress signaling pathway, disturbed transcriptional regulation, and impaired intracellular homeostasis and cytoskeletal stability, thereby synergistically suppressing the expression of key byssal protein genes including mfp-1 and mfp-3 and ultimately blocking byssus synthesis and adhesion. This study clarifies the multi-pathway molecular mechanism underlying antifouling agent-induced attachment inhibition in M. edulis, and provides core molecular targets and theoretical support for developing efficient, specific antifouling activity, and potentially applicable marine antifouling technologies.

Animals↗
PubMed1999

Tissue-specific heavy metal (Cd, Pb, Cu, Zn) deposition in a natural population of the zebra mussel Dreissena polymorpha Pallas.

The zebra mussel Dreissena polymorpha was tested as an indicator of heavy metal exposure in urban waters of Vienna, Austria. Mussels, two sediment fractions, suspended matter, and filtrate were collected over one annual cycle at five sampling stations. Dreissena was dissected into five body parts: viscera, gill, foot, byssus, and shell, to determine tissue-specific metal accumulation. Cadmium, lead, copper, and zinc were measured by AAS. There was no clear relationship between (relatively low) metal concentrations in ambient compartments and in zebra mussel bodies. Therefore, D. polymorpha must be regarded as a poor suitable indicator tool under near-background contamination situations. Tissue-specific metal accumulation showed that cadmium was mainly stored in soft body parts. Lead, copper, and zinc showed significantly highest concentrations in the byssal threads. Metal concentrations and distribution patterns within the mussel's body must be interpreted as a result of (unknown) internal metal treatment/regulation. Excretion of lead, copper, and zinc via the byssus complex probably is an effective strategy for preventing toxic injury in D. polymorpha.

Animals↗
PubMed2002

Influence of temperature on the physiological responses of the bivalve Brachidontes striatulus and its significance in fouling control.

Heat treatment offers an alternative method of fouling control to chlorination in power plants. In order to optimise such a procedure it is important to understand the responses of fouling organisms to elevated water temperatures. In this paper we report results of experiments on the lethal and sub-lethal effects of temperature on the bivalve Brachidontes striatulus which is one of the major foulants in the process seawater heat exchangers of Madras Atomic Power Station located at Kalpakkam, on the east coast of India. The important physiological activities, such as, oxygen consumption, filtration rate, byssus thread production and faecal matter production were studied at temperatures varying from 20 to 38 degrees C. Three different size groups [3-5 mm shell length (group 1), 6-10 mm (group 2), 11-15 mm (group 3)] of B. striatulus were used for the experiments. The results showed physiological activities were maximum at 35 degrees C, minimum at 20 and 38 degrees C. Physiological activities increased with size except for byssus thread production, which did not show any trend. Survival times showed a reduction from 30 h at 39 degrees C to < 1 h at 45 degrees C and were independent of body size.

Adaptation, Physiological↗
PubMed2000

Development of an antagonist of molluscan neuropeptide APGWamide with a peptide library.

Fifty-seven kinds of APGWamide-related peptides and a peptide library consisting of 38 peptide mixtures, each of which contained 19 kinds of APGWamide-related peptides, were synthesized with a multipeptide synthesizer, and their APGWamide-agonistic or -antagonistic effects were examined on the anterior byssus retractor muscle of the bivalve Mytilus edulis and the crop of the land snail Euhadra congenita. The peptide mixtures having agonistic or antagonistic effects were subjected to HPLC purification to isolate the active peptides using the muscles as bioassay systems. Many peptides having agonistic or antagonistic effects were obtained. Of the antagonists, APGWGNamide, isolated from the peptide mixture of APGWGXamide, was the most potent. At 10(-4) M, APGWGNamide almost completely blocked the actions of 10(-6) M APGWamide on the anterior byssus retractor muscle of M. edulis and the crop of E. congenita.

Animals↗
PubMed2003

Green mussel Perna viridis L.: attachment behaviour and preparation of antifouling surfaces.

The green mussel Perna viridis LINNE can be kept in simulated seawater for more than 6 months in good condition. The mussel forms many threads by secreting an adhesive protein from the foot, and attaches with more than 50 byssal threads, which makes most mussels clump together. In order to investigate the preparation of the antifouling surfaces toward green mussels, the attachment of mussels was tested using glass surfaces modified with silane coupling agents, together with non-treated material surfaces such as glass and silicone. The correlation between the attachment percentage and the mean number of the secreted byssus was highly significant, indicating that the mussel selects a favorable surface prior to the secretion of byssus. The relationships between the mussel attachment and the surface chemical parameters (surface free energy (sfe) and its dispersion and polar components) were examined based on a working hypothesis, which we have previously reported. The result of statistical regression test indicated that a certain correlation was found between the dispersion component and the mussel attachment, while the polar component did not correlate to the mussel attachment. The present surface chemical approach provided an additional clue for the preparation of ecologically clean antifouling materials that takes into account the combination of the wettability of both the marine adhesive proteins (MAP) and the modified surfaces.

Animals↗
PubMed2000

Cross-linking in adhesive quinoproteins: studies with model decapeptides.

Mytilus edulis foot protein-1 (mefp1) is a major component of the byssus, an adhesive holdfast in mussels. The recent report of 5, 5'-di(dihydroxyphenyl-L-alanine) (diDOPA) cross-links in byssus [McDowell et al. (1999) J. Biol. Chem. 274, 20293] has raised questions about the relationship of these to mefp1. About 80% of the primary structure of mefp1 consists of a tandemly repeated consensus sequence Ala(1)-Lys(2)-Pro(3)-Ser(4)-Tyr(5)-Pro(6)-Pro(7)-Thr(8)-Tyr(9)-Lys(10 ) with varying degrees of posttranslational hydroxylation to hydroxyprolines in positions 3, 6, and 7 and to DOPA in positions 5 and 9. Six natural or synthetic variants of this decapeptide were subjected to oxidation by tyrosinase or periodate. DOPA is the only residue to suffer losses in all oxidized peptides. Moreover, using MALDI TOF mass spectrometry, oxidized decapeptides all showed evidence of multimer formation and a mass loss of 6 Da per coupled pair of peptides. Multimer formation was inhibited by addition of DOPA-like o-diphenols, but addition of simple amines such as free Lys had no effect. The results are consistent with aryloxy coupling to diDOPA followed by reoxidation to diDOPA quinone. There are subtle but noteworthy variations, however, in multimer formation among the peptide congeners. Decapeptides with Pro(3) modified to trans-4-hydroxyproline do not form multimers beyond dimers; they also exhibit significant Lys losses following oxidation of DOPA. Moreover, in Ala-Lys-Hyp-Ser-Tyr-DiHyp-Hyp-Thr-DOPA-Lys, Tyr appears to be protected from oxidation by tyrosinase.

Adhesiveness↗
PubMed2005

Coating proteins: structure and cross-linking in fp-1 from the green shell mussel Perna canaliculus.

The protein family known as fp-1 provides mussel byssus with a protective outer coating and has drawn much attention for its water resistant bioadhesive properties in vitro. A new fp-l isolated from the green shell mussel Perna canaliculus (pcfp-1) reveals a composition dominated by only four amino acids: 3,4-dihydroxyphenyl-L-alanine (dopa), lysine, proline, and valine at approximately 20 mol % each. SDS-PAGE and MALDI-TOF mass spectrometry detected size variants at 48 and 52 kDa in preparations of purified Pcfp-1. The N-terminal sequence enabled construction of oligonucleotide primers for PCR and RACE-derived cDNAs from which the complete sequence of four variants was deduced. pcfp-1 deviates from all known homologues in other mussels in several notable respects: its mass is half, most of its sequence is represented by 75 tandem repeats of a tetrapeptide, i.e., PY*VK, in which Y* is dopa, prolines are not hydroxylated, and thiolate cysteines are clustered in homologous sequences at both the amino and carboxy termini. Amino acids in the repeat sequence show a striking resemblance to proline-rich cell wall proteins with tandemly repeated PPVYK pentapeptides [Hong, J. C., Nagao, R. T., and Key, J. L. (1987) J. Biol. Chem. 262, 8367-8376]. Cysteine plays a key role in cross-linking pcfp-1 by forming adducts with dopaquinone. Significant 5-S-cysteinyldopa and smaller amounts of 2-S-cysteinyldopa were detected in hydrolysates of the byssal threads of P. canaliculus. The cross-links could also be formed by oxidation of pcfp-1 in vitro using mushroom tyrosinase. Cysteinyldopa cross-links were present in trace amounts only in the byssus of other mussel species.

Adhesiveness↗
PubMed2002

Elastomeric gradients: a hedge against stress concentration in marine holdfasts?

The byssal threads of marine mussels are elastomeric fibres with a great capacity for absorbing and dissipating energy. Up to 70% of the total absorbed energy can be dissipated in the byssus. Because byssal threads attach the mussel to hard inert surfaces in its habitat, they must combine the need to be good shock absorbers with appropriate matching of Young's modulus between living tissue and a hard sub-stratum such as stone - stiffnesses that can differ by five orders of magnitude. Recent data suggest that improved modulus matching and decreased stress concentration between different portions of the byssus is achieved by the use of protein gradients. Protein gradients in byssal threads are constructed using natural macromolecular chimeras having a central collagenous domain, variable flanking modules and histidine-rich amino and carboxy termini. Stiff silk-like flanking modules prevail distally, while at the animal end, rubbery modules resembling elastin predominate. In between the two thread ends there is a mix of both module types. The histidine-rich termini provide metal binding/cross-linking sites, while collagen domains may confer self-assembly on all parts of the structure. A graded axial distribution of flanking modules is expected to moderate stress concentration in joined materials having disparate moduli.

Amino Acid Sequence↗