Functional analysis of Pacific oyster (Crassostrea gigas) β-thymosin: Focus on antimicrobial activity

Nam, Bo‐Hye; Seo, Jung-Kil; Lee, Min Jeong; Kim, Young‐Ok; Kim, Dong-Gyun; An, Cheul Min; Park, Nam Gyu

doi:10.1016/j.fsi.2015.03.035

Cited by 39 publications

(36 citation statements)

References 26 publications

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“…β-thymosins, which were originally isolated from calf thymus, are widely expressed in vertebrates, and their isoforms and multi-repeat β-thymosins have been found in invertebrates, including crustaceans (Vancompernolle et al, 1991;Safer and Chowrashi, 1997;Boquet et al, 2000;Crow and Xue-Bian, 2000;Huff et al, 2001;Van Troys et al, 2004;Herrmann et al, 2005;Romanova et al, 2006;Gai et al, 2009;Wu and Wu, 2009;Kasthuri et al, 2013;Nam et al, 2015;Shi et al, 2015). It is well-known that β-thymosin mainly possesses intracellular actin binding activities; several extracellular activities have also been identified in the antimicrobial process, tissue repair, inflammation response, wound-healing, cell mediated immune response, antiviral immunity (Gai et al, 2009;Choi et al, 2011;Zhu et al, 2014;Shi et al, 2015;Xiao et al, 2015).…”

Section: Discussionmentioning

confidence: 99%

“…Sequence analysis indicated that mjthm4, mjthm3, and mjthm2 proteins belong to the β-thymosin family of protein, as their predicted pIs were all between 5.0 and 7.0, which is characteristic of β-thymosins. This suggests that mjthm4, mjthm3, and mjthm2 are novel multi-repeat β-thymosins in shrimps and that they might represent a divergent group that possesses multi-repeat β-thymosin patterns (Vancompernolle et al, 1991;Boquet et al, 2000;Crow and Xue-Bian, 2000; Van Troys Herrmann et al, 2005;Gai et al, 2009;Kasthuri et al, 2013;Nam et al, 2015;Shi et al, 2015). The three β-thymosin proteins contained six different β-thymosin actin binding modules, and these modules possessed an LKxxxTxEK motif and four modules had a KExxExEK motif at the C-terminal end, which might explain the different functions for mjthm4, mjthm3, and mjthm2.…”

Section: Figmentioning

confidence: 99%

“…α-thymosins have a pI below 5.0, β-thymosins have a pI between 5.0 and 7.0, and γ-thymosins have a pI above 7.0. β-thymosin or G-actin sequestering peptides have been found in various vertebrates (Huff et al, 2001). As intracellular structural elements and extracellular fluids, they contain a single conserved β-thymosin domain and play an important role in various vital biological processes such as angiogenesis (Dettin et al, 2011;Lv et al, 2013), inflammation response (Choi et al, 2011), wound-healing (Sosne et al, 2010;Zhu et al, 2014), repair and regeneration (Bollini et al, 2015), antimicrobial activity (Nam et al, 2015), cell mediated immune response (Xiao et al, 2015). In contrast, invertebrates such as Acanthamoeba Actobindin (Vancompernolle et al, 1991), Hydra Thypedin (Herrmann et al, 2005), Caenorhabditis Tetra Thymosinβ (Van Troys et al, 2004), Hermissenda Csp24 (Crow and XueBian, 2000), Eriocheir EsTRP1 and EsTRP2 (Gai et al, 2009), and Drosophila Cibulout (Boquet et al, 2000), Procambarus clarkia PcThy-1 to PcThy-1 (Shi et al, 2015), usually have β-thymosins with multi-β-thymosin domains.…”

Section: Introductionmentioning

confidence: 99%

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Molecular characteristics of three thymosin-repeat proteins from Marsupenaeus japonicus and their responses to WSSV infection

Ruan

et al. 2016

Acta Oceanol. Sin.

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β-thymosins, a family of highly conserved peptides, play a vital role in wound-healing, angiogenesis, antimicrobial process and antiviral immunity. Three novel β-thymosin-repeat proteins, named mjthm4, mjthm3 and mjthm2, were cloned from Marsupenaeus japonicus using expressed sequence tags (EST) from suppression subtractive hybridization. The mjthm4, mjthm3 and mjthm2 cDNAs possessed open reading frames that encoded 166, 128 and 90 amino acid residue polypeptides and contained four, three and two β-thymosin actin binding modules, respectively. Blast analysis demonstrated that mjthm4, mjthm3 and mjthm2 shared high homology with known invertebrate multi-repeat β-thymosins. These proteins are ubiquitously expressed in all of the examined tissues, and the transcriptional levels were highest in the intestine. Further investigation revealed that mjthm4, mjthm3 and mjthm2 were remarkably up-regulated 6 h after WSSV infection. Moreover, while mjthm4 transcriptional levels displayed no changes, mjthm3 and mjthm2 levels decreased in the virus-resistant shrimps.The results indicate that mjthm4, mjthm3 and mjthm2 are novel multi-repeat β-thymosin homologues, have a close relationship with WSSV infection, and might contribute to a better understanding of host defense and/or virus invasion interactions in shrimps. Citation: Ma Jinyou, Ruan Lingwei, Xu Xun, Gao Zhaoming. 2016. Molecular characteristics of three thymosin-repeat proteins from Marsupenaeus japonicus and their responses to WSSV infection. Acta Oceanologica Sinica, 35(4): 44-50,

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Section: Discussionmentioning

confidence: 99%

Section: Figmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Molecular characteristics of three thymosin-repeat proteins from Marsupenaeus japonicus and their responses to WSSV infection

Ruan

et al. 2016

Acta Oceanol. Sin.

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“…Bercangkang Tebal Metode ekstraksi daging gonggong Bintan mengacu pada modifikasi Ali et al (2006) dan Nam et al (2015). Daging gonggong rebus bercangkang tebal dipilih untuk diekstraksi karena berdasarkan uji hedonik terhadap gonggong bercangkang tipis dan gonggong tebal didapatkan bahwa masyarakat dan wisatawan lebih menyukai gonggong rebus bercangkang tebal (Viruly, 2011).…”

Section: Ekstraksi Daging Gonggong Rebusunclassified

“…dan lain-lain. Fakta-fakta tersebut dapat menyebabkan perbedaan dalam profil protein pada suatu spesies (Nam et al, 2015;Cob et al, 2009b;Duval et al, 2009). Respon metamorfosis larva gonggong sangat dipengaruhi oleh sedimen dan substrata detrital sebagai makanan gonggong dari habitat alami yang memungkinkan perbedaan jenis protein gonggong yang bermutasi karena untuk mempertahankan diri (Cob et al, 2010;Duval et al, 2009).…”

Section: Gambar 2 Profil Protein Pada Lendirunclassified

PROTEIN HISTON PADA SIPUT GONGGONG BINTAN Strombus sp. SEBAGAI KANDIDAT PANGAN FUNGSIONAL

Viruly

Andarwulan

Suhartono³

et al. 2019

J. Ilmu dan Teknologi Kelautan Tropis

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ABSTRAKGonggong termasuk sejenis siput laut, biota endemik yang banyak hidup di pantai Pulau Bintan dan sekitarnya di Provinsi Kepulauan Riau. Gonggong merupakan ikon kota Tanjungpinang, Provinsi Kepulauan Riau. Sampai saat ini, penelitian gonggong masih sangat sedikit padahal siput ini merupakan spesies yang sangat potensial. Tujuan penelitian ini adalah untuk mengkarakterisasi protein histon dari siput gonggong Strombus sp. asal Bintan sebagai kandidat pangan fungsional. Karakterisasi profil protein menggunakan SDS-PAGE. Kadar protein pada gonggong dianalisis dengan menggunakan metode Bradford. Gonggong rebus bercangkang tebal diekstraksi dengan metode maserasi menggunakan pelarut etanol PA 95% dan uji aktivitas antimikroba menggunakan metode sumur. Asam amino dianalisis menggunakan HPLC. Hasil karakterisasi profil protein pada daging gonggong menunjukkan bahwa gonggong bercangkang tipis dan gonggong bercangkang tebal memiliki pita profil protein yang sama pada berat molekul 11-37 kDa, sedangkan profil protein pada lendir gonggong bercangkang tebal dan tipis memiliki pita protein yang sama pada berat molekul 37 kDa. Jenis protein pada spesies gonggong Bintan diprediksi merupakan protein histon karena hasil amplifikasi menggunakan primer protein histon H2A dan H2B didapatkan gen target pada 75 bp dan uji antimikroba pada bakteri S. aureus dan E. coli memiliki nilai DDH sebesar 25,65±0,02 mm dan 14,45±0,13 mm, sehingga diduga bahwa gonggong Bintan berpotensi sebagai kandidat pangan fungsional khas Kepulauan Riau. ABSTRACTGonggong is one of the sea snails, endemic species living on coastal waters of Bintan Island and surrounding islands of the Riau Islands Province. Sea snail gonggong is an icon of Tanjungpinang-Riau Islands Province. Until now, research this snail is the least, whereas it is potential species. The purpose of this study was to characterize histone protein from Bintan gonggong snail Strombus sp. as functional food candidate. Protein profiling used SDS-PAGE. Protein contents were analyzed by Bradford method. Boiled thick shelled gonggong were extracted by maseration method using ethanol PA 95% and antimicrobial activity tes using well method. Amino acid analized with HPLC. The result of characterization on protein profiles in meat gonggong showed that the thin-shelled and thick-shelled gonggong had the same band as protein profiles by 11-37 kDa and protein profiles in mucus gonggong were found the same band as protein profiles of 37 kDa. The type of protein in spesies Bintan gonggong had been predicted a histone protein because DNA identification using primer protein histone H2A and H2B had gen target of 75 bp. Antimicrobial activity test on S. aureus and E. coli bacteria had value DDH of 25.65±0.02 mm and 14.45±0.13 mm. In fact, gonggong snail was potentially as antimicrobial peptide, so it will make local functional food candidate from Riau Islands Province.

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Semi-purified Antimicrobial Proteins from Oyster Hemolymph Inhibit Pneumococcal Infection

Summer,

Liu,

Guo

et al. 2024

Mar Biotechnol

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Pneumococcal infections caused by Streptococcus pneumoniae are a leading cause of morbidity and mortality globally, particularly among children. The ability of S. pneumoniae to form enduring biofilms makes treatment inherently difficult, and options are further limited by emerging antibiotic resistance. The discovery of new antibiotics, particularly those with antibiofilm activity, is therefore increasingly important. Antimicrobial proteins and peptides (AMPs) from marine invertebrates are recognised as promising pharmacological leads. This study determined the in vitro antibacterial activity of hemolymph and unique protein fractions from an Australian oyster (Saccostrea glomerata) against multi-drug-resistant S. pneumoniae. We developed a successful method for hemolymph extraction and separation into 16 fractions by preparative HPLC. The strongest activity was observed in fraction 7: at 42 µg/mL protein, this fraction was bactericidal to S. pneumoniae and inhibited biofilm formation. Proteomic analysis showed that fraction 7 contained relatively high abundance of carbonic anhydrase, cofilin, cystatin B–like, and gelsolin-like proteins, while surrounding fractions, which showed lower or no antibacterial activity, contained these proteins in lower abundance or not at all. This work supports traditional medicinal uses of oysters and contributes to further research and development of novel hemolymph/AMP-based treatments for pneumococcal infections.

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Functional analysis of Pacific oyster (Crassostrea gigas) β-thymosin: Focus on antimicrobial activity

Cited by 39 publications

References 26 publications

Molecular characteristics of three thymosin-repeat proteins from Marsupenaeus japonicus and their responses to WSSV infection

Molecular characteristics of three thymosin-repeat proteins from Marsupenaeus japonicus and their responses to WSSV infection

PROTEIN HISTON PADA SIPUT GONGGONG BINTAN Strombus sp. SEBAGAI KANDIDAT PANGAN FUNGSIONAL

Semi-purified Antimicrobial Proteins from Oyster Hemolymph Inhibit Pneumococcal Infection

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