Biopolymers from Marine Invertebrates. XIII. Characterization of an Antibacterial Protein, Dolabellanin A, from the Albumen Gland of the Sea Hare, Dolabella auricularia.

Kisugi, Jun; Ohye, Hirokazu; Kamiya, Hisao; Yamazaki, Masatoshi

doi:10.1248/cpb.40.1537

Cited by 19 publications

(6 citation statements)

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“…Dolabella auricularia is another anaspidean known for protecting their eggs from bacterial pathogens, with a de novo biosynthesized glycoprotein, dolabellanin A, located in the albumen gland, showing antibacterial activity [ 435 ].…”

Section: Ecological Activitymentioning

confidence: 99%

“…As mentioned above, Dolabella auricularia , possesses the glycoprotein dolabellanin A, probably de novo biosynthesized [ 435 ]. Besides its antineoplastic activity, dolabellanin A also shows antibacterial activity against E. coli , which may protect the egg masses from bacterial pathogens [ 435 ].…”

Section: Pharmacological Activitymentioning

confidence: 99%

“…Moreover, the cosmopolitan Aplysia juliana presents two toxic chlorophyll derivatives, pyropheophorbides a and b, and a halogenated diterpenoid lactone, while its purple secretion also includes an antibacterial and cytotoxic peptide, julianin-S, and their egg masses are protected from microbial infections by unsaturated fatty acids [288,[432][433][434]. Dolabella auricularia is another anaspidean known for protecting their eggs from bacterial pathogens, with a de novo biosynthesized glycoprotein, dolabellanin A, located in the albumen gland, showing antibacterial activity [435].…”

Section: Anaspideamentioning

confidence: 99%

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Bioactive Compounds from Marine Heterobranchs

Ávila

Angulo‐Preckler

2020

Marine Drugs

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The natural products of heterobranch molluscs display a huge variability both in structure and in their bioactivity. Despite the considerable lack of information, it can be observed from the recent literature that this group of animals possesses an astonishing arsenal of molecules from different origins that provide the molluscs with potent chemicals that are ecologically and pharmacologically relevant. In this review, we analyze the bioactivity of more than 450 compounds from ca. 400 species of heterobranch molluscs that are useful for the snails to protect themselves in different ways and/or that may be useful to us because of their pharmacological activities. Their ecological activities include predator avoidance, toxicity, antimicrobials, antifouling, trail-following and alarm pheromones, sunscreens and UV protection, tissue regeneration, and others. The most studied ecological activity is predation avoidance, followed by toxicity. Their pharmacological activities consist of cytotoxicity and antitumoral activity; antibiotic, antiparasitic, antiviral, and anti-inflammatory activity; and activity against neurodegenerative diseases and others. The most studied pharmacological activities are cytotoxicity and anticancer activities, followed by antibiotic activity. Overall, it can be observed that heterobranch molluscs are extremely interesting in regard to the study of marine natural products in terms of both chemical ecology and biotechnology studies, providing many leads for further detailed research in these fields in the near future.

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Section: Ecological Activitymentioning

confidence: 99%

Section: Pharmacological Activitymentioning

confidence: 99%

Section: Anaspideamentioning

confidence: 99%

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Bioactive Compounds from Marine Heterobranchs

Ávila

Angulo‐Preckler

2020

Marine Drugs

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“…Antimicrobial peptides and proteins are important components of the innate defense in all species investigated [1]. Several peptides with antibacterial effect against various Gram‐positive and Gram‐negative bacteria have been isolated from marine invertebrates including horseshoe crab [2], shore crab [3] and mollusks [4,5], and antibacterial proteins have been isolated from sea hare [6,7] and from bivalve mollusks [8]. Marine bivalves are filter feeders and free‐living bacteria are one of their major sources of nutrition.…”

Section: Introductionmentioning

confidence: 99%

Protein purification and gene isolation of chlamysin, a cold‐active lysozyme‐like enzyme with antibacterial activity

Nilsen¹,

Øverbø²,

Sandsdalen³

et al. 1999

FEBS Letters

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An antibacterial V V11 kDa protein designated chlamysin was isolated from viscera of the marine bivalve Chlamys islandica. Chlamysin inhibited the growth of all Grampositive and Gram-negative bacteria tested. The isolated protein was highly efficient in hydrolyzing Micrococcus luteus cells only at low pH (4.5^6.2) and at low temperature (4^35³C). No significant loss of enzyme activity was observed after 30 days storage at room temperature or after heating to 70³C for 15 min, suggesting relatively high protein structure stability. Sequenceanalyzed fragments of the protein revealed data which guided the isolation of the cDNA gene, encoding a 137 amino acid chlamysin precursor in scallops. The deduced protein contains a high portion of cysteine, serine and histidine residues and has a predicted isoelectric point below 7. The chlamysin protein was found to have sequence homology to an isopeptidase and to a recently published bivalve lysozyme.z 1999 Federation of European Biochemical Societies.

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“…Antibacterial peptides/proteins which are different in physiological and biochemical characteristics such as molecular mass, MIC and antibacterial spectrum have been isolated from a variety of organisms. Kisugi et al (1992) purified from Dolabella auricularia a large, 250-kDa antibacterial glycoprotein consisting of four subunits and showing both antibacterial and antineoplastic activities. Another large antibacterial protein of 190-kDa was isolated from Ciona intestinalis.…”

Section: Discussionmentioning

confidence: 99%

Purification and characterization of an antibacterial protein from dried fruiting bodies of the wild mushroom Clitocybe sinopica.

Zheng¹,

Liu²,

Zhang³

et al. 2010

Acta Biochim Pol

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A novel antibacterial protein with a molecular mass of 44 kDa has been isolated from dried fruiting bodies of the wild mushroom Clitocybe sinopica. Sodium dodecyl sulfate/polyacrylamide gel electrophoresis showed that the protein was composed of two subunits each with a molecular mass of 22 kDa. Its N-terminal amino-acid sequence, SVQATVNGDKML, has not been reported for other antimicrobial proteins. The purification protocol included ion exchange chromatography on DEAE-cellulose, CM-cellulose and Q-Sepharose, and gel filtration by fast protein liquid chromatography on Superdex 75. The antibacterial protein was adsorbed on all three ion exchangers. The antimicrobial activity profile of the protein against tested bacterial and fungal strains disclosed that it possessed potent antibacterial activity against Agrobacterium rhizogenes, A. tumefaciens, A. vitis, Xanthomonas oryzae and X. malvacearum with a minimum inhibitory concentration mostly below 0.6 microM. However, it had no antibacterial activity against Pseudomonas batatae, Erwinia herbicola, Escherichia coli, and Staphylococcus aureus, and no antifungal activity against Setosphaeria turcica, Fusarium oxysporum, Verticillium dahliae, Bipolaris maydis, and B. sativum. The antibacterial antivity against A. tumefaciens was stable after exposure to 20-60 degrees C for 30 min and to pH 4-9 for 1 h.

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Biopolymers from Marine Invertebrates. XIII. Characterization of an Antibacterial Protein, Dolabellanin A, from the Albumen Gland of the Sea Hare, Dolabella auricularia.

Cited by 19 publications

References 1 publication

Bioactive Compounds from Marine Heterobranchs

Bioactive Compounds from Marine Heterobranchs

Protein purification and gene isolation of chlamysin, a cold‐active lysozyme‐like enzyme with antibacterial activity

Purification and characterization of an antibacterial protein from dried fruiting bodies of the wild mushroom Clitocybe sinopica.

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