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Lilibeth A. Salvador-Reyes
Marine Science Institute, University of the Philippines- Diliman, Velasquez St., Quezon City 1101, Philippines

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Journal article
Published: 23 December 2020 in Toxins
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Alexandrium minutum and Alexandrium tamutum are two closely related harmful algal bloom (HAB)-causing species with different toxicity. Using isobaric tags for relative and absolute quantitation (iTRAQ)-based quantitative proteomics and two-dimensional differential gel electrophoresis (2D-DIGE), a comprehensive characterization of the proteomes of A. minutum and A. tamutum was performed to identify the cellular and molecular underpinnings for the dissimilarity between these two species. A total of 1,436 proteins and 420 protein spots were identified using iTRAQ-based proteomics and 2D-DIGE, respectively. Both methods revealed little difference (10-12%) between the proteomes of A. minutum and A. tamutum, highlighting that these organisms follow similar cellular and biological processes at the exponential stage. Toxin biosynthetic enzymes were present in both organisms. However, the gonyautoxin-producing A. minutum showed higher levels of osmotic growth proteins, Zn-dependent alcohol dehydrogenase and type-I polyketide synthase compared to the non-toxic A. tamutum. Further, A. tamutum had increased S-adenosylmethionine transferase that may potentially have a negative feedback mechanism to toxin biosynthesis. The complementary proteomics approach provided insights into the biochemistry of these two closely related HAB-causing organisms. The identified proteins are potential biomarkers for organismal toxicity and could be explored for environmental monitoring.

ACS Style

Bryan John J. Subong; Arturo O. Lluisma; Rhodora V. Azanza; Lilibeth A. Salvador-Reyes. Differentiating Two Closely Related Alexandrium Species Using Comparative Quantitative Proteomics. Toxins 2020, 13, 7 .

AMA Style

Bryan John J. Subong, Arturo O. Lluisma, Rhodora V. Azanza, Lilibeth A. Salvador-Reyes. Differentiating Two Closely Related Alexandrium Species Using Comparative Quantitative Proteomics. Toxins. 2020; 13 (1):7.

Chicago/Turabian Style

Bryan John J. Subong; Arturo O. Lluisma; Rhodora V. Azanza; Lilibeth A. Salvador-Reyes. 2020. "Differentiating Two Closely Related Alexandrium Species Using Comparative Quantitative Proteomics." Toxins 13, no. 1: 7.

Journal article
Published: 20 December 2020 in Marine Drugs
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The bioactivity-guided purification of the culture broth of the shipworm endosymbiont Teredinibacter turnerae strain 991H.S.0a.06 yielded a new fatty acid, turneroic acid (1), and two previously described oxylipins (2–3). Turneroic acid (1) is an 18-carbon fatty acid decorated by a hydroxy group and an epoxide ring. Compounds 1–3 inhibited bacterial biofilm formation in Staphylococcus epidermidis, while only 3 showed antimicrobial activity against planktonic S. epidermidis. Comparison of the bioactivity of 1–3 with structurally related compounds indicated the importance of the epoxide moiety for selective and potent biofilm inhibition.

ACS Style

Noel M. Lacerna; Cydee Marie V. Ramones; Jose Miguel D. Robes; Myra Ruth D. Picart; Jortan O. Tun; Bailey W. Miller; Margo G. Haygood; Eric W. Schmidt; Lilibeth A. Salvador-Reyes; Gisela P. Concepcion. Inhibition of Biofilm Formation by Modified Oxylipins from the Shipworm Symbiont Teredinibacter turnerae. Marine Drugs 2020, 18, 656 .

AMA Style

Noel M. Lacerna, Cydee Marie V. Ramones, Jose Miguel D. Robes, Myra Ruth D. Picart, Jortan O. Tun, Bailey W. Miller, Margo G. Haygood, Eric W. Schmidt, Lilibeth A. Salvador-Reyes, Gisela P. Concepcion. Inhibition of Biofilm Formation by Modified Oxylipins from the Shipworm Symbiont Teredinibacter turnerae. Marine Drugs. 2020; 18 (12):656.

Chicago/Turabian Style

Noel M. Lacerna; Cydee Marie V. Ramones; Jose Miguel D. Robes; Myra Ruth D. Picart; Jortan O. Tun; Bailey W. Miller; Margo G. Haygood; Eric W. Schmidt; Lilibeth A. Salvador-Reyes; Gisela P. Concepcion. 2020. "Inhibition of Biofilm Formation by Modified Oxylipins from the Shipworm Symbiont Teredinibacter turnerae." Marine Drugs 18, no. 12: 656.

Journal article
Published: 07 August 2020 in Toxins
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The cone snails (family Conidae) are the best known and most intensively studied venomous marine gastropods. However, of the total biodiversity of venomous marine mollusks (superfamily Conoidea, >20,000 species), cone snails comprise a minor fraction. The venoms of the family Drilliidae, a highly diversified family in Conoidea, have not previously been investigated. In this report, we provide the first biochemical characterization of a component in a Drilliidae venom and define a gene superfamily of venom peptides. A bioactive peptide, cdg14a, was purified from the venom of Clavus davidgilmouri Fedosov and Puillandre, 2020. The peptide is small (23 amino acids), disulfide-rich (4 cysteine residues) and belongs to the J-like drillipeptide gene superfamily. Other members of this superfamily share a conserved signal sequence and the same arrangement of cysteine residues in their predicted mature peptide sequences. The cdg14a peptide was chemically synthesized in its bioactive form. It elicited scratching and hyperactivity, followed by a paw-thumping phenotype in mice. Using the Constellation Pharmacology platform, the cdg14a drillipeptide was shown to cause increased excitability in a majority of non-peptidergic nociceptors, but did not affect other subclasses of dorsal root ganglion (DRG) neurons. This suggests that the cdg14a drillipeptide may be blocking a specific molecular isoform of potassium channels. The potency and selectivity of this biochemically characterized drillipeptide suggest that the venoms of the Drilliidae are a rich source of novel and selective ligands for ion channels and other important signaling molecules in the nervous system.

ACS Style

Victor M. Chua; Joanna Gajewiak; Maren Watkins; Samuel S. Espino; Iris Bea L. Ramiro; Carla A. Omaga; Julita S. Imperial; Louie Paolo D. Carpio; Alexander Fedosov; Helena Safavi-Hemami; Lilibeth A. Salvador-Reyes; Baldomero M. Olivera; Gisela P. Concepcion. Purification and Characterization of the Pink-Floyd Drillipeptide, a Bioactive Venom Peptide from Clavus davidgilmouri (Gastropoda: Conoidea: Drilliidae). Toxins 2020, 12, 508 .

AMA Style

Victor M. Chua, Joanna Gajewiak, Maren Watkins, Samuel S. Espino, Iris Bea L. Ramiro, Carla A. Omaga, Julita S. Imperial, Louie Paolo D. Carpio, Alexander Fedosov, Helena Safavi-Hemami, Lilibeth A. Salvador-Reyes, Baldomero M. Olivera, Gisela P. Concepcion. Purification and Characterization of the Pink-Floyd Drillipeptide, a Bioactive Venom Peptide from Clavus davidgilmouri (Gastropoda: Conoidea: Drilliidae). Toxins. 2020; 12 (8):508.

Chicago/Turabian Style

Victor M. Chua; Joanna Gajewiak; Maren Watkins; Samuel S. Espino; Iris Bea L. Ramiro; Carla A. Omaga; Julita S. Imperial; Louie Paolo D. Carpio; Alexander Fedosov; Helena Safavi-Hemami; Lilibeth A. Salvador-Reyes; Baldomero M. Olivera; Gisela P. Concepcion. 2020. "Purification and Characterization of the Pink-Floyd Drillipeptide, a Bioactive Venom Peptide from Clavus davidgilmouri (Gastropoda: Conoidea: Drilliidae)." Toxins 12, no. 8: 508.

Journal article
Published: 16 September 2019 in Marine Drugs
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Renieramycin M (RM) is a KCN-stabilized tetrahydroisoquinoline purified from the blue sponge Xestospongia sp., with nanomolar IC50s against several cancer cell lines. Our goal is to evaluate its combination effects with doxorubicin (DOX) in estrogen receptor positive MCF-7 breast cancer cells. MCF-7 cells were treated simultaneously or sequentially with various combination ratios of RM and DOX for 72 h. Cell viability was determined using the MTT assay. Synergism or antagonism was determined using curve-shift analysis, combination index method and isobologram analysis. Synergism was observed with pharmacologically achievable concentrations of DOX when administered simultaneously, but not sequentially. The IC95 values of RM and DOX after combination were reduced by up to four-fold and eight-fold, respectively. To gain insights on the mechanism of synergy, real-time profiling, cell cycle analysis, apoptosis assays, and transcriptome analysis were conducted. The combination treatment displayed a similar profile with DNA-damaging agents and induced a greater and faster cell killing. The combination treatment also showed an increase in apoptosis. DOX induced S and G2/M arrest while RM did not induce significant changes in the cell cycle. DNA replication and repair genes were downregulated commonly by RM and DOX. p53 signaling and cell cycle checkpoints were regulated by DOX while ErbB/PI3K-Akt, integrin and focal adhesion signaling were regulated by RM upon combination. Genes involved in cytochrome C release and interferon gamma signaling were regulated specifically in the combination treatment. This study serves as a basis for in vivo studies and provides a rationale for using RM in combination with other anticancer drugs.

ACS Style

Jortan O. Tun; Lilibeth A. Salvador-Reyes; Michael C. Velarde; Naoki Saito; Khanit Suwanborirux; Gisela P. Concepcion. Synergistic Cytotoxicity of Renieramycin M and Doxorubicin in MCF-7 Breast Cancer Cells. Marine Drugs 2019, 17, 536 .

AMA Style

Jortan O. Tun, Lilibeth A. Salvador-Reyes, Michael C. Velarde, Naoki Saito, Khanit Suwanborirux, Gisela P. Concepcion. Synergistic Cytotoxicity of Renieramycin M and Doxorubicin in MCF-7 Breast Cancer Cells. Marine Drugs. 2019; 17 (9):536.

Chicago/Turabian Style

Jortan O. Tun; Lilibeth A. Salvador-Reyes; Michael C. Velarde; Naoki Saito; Khanit Suwanborirux; Gisela P. Concepcion. 2019. "Synergistic Cytotoxicity of Renieramycin M and Doxorubicin in MCF-7 Breast Cancer Cells." Marine Drugs 17, no. 9: 536.

Journal article
Published: 09 August 2019 in Toxins
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Bivalve molluscs represent an important food source within the Philippines, but the health of seafood consumers is compromised through the accumulation of harmful algal toxins in edible shellfish tissues. In order to assess the dynamics of toxin risk in shellfish, this study investigated the uptake, depuration, assimilation, and analogue changes of paralytic shellfish toxins in Perna viridis. Tank experiments were conducted where mussels were fed with the toxic dinoflagellate Alexandrium minutum. Water and shellfish were sampled over a six day period to determine toxin concentrations in the shellfish meat and water, as well as algal cell densities. The maximum summed toxin concentration determined was 367 µg STX eq./100 g shellfish tissue, more than six times higher than the regulatory action limit in the Philippines. Several uptake and depuration cycles were observed during the study, with the first observed within the first 24 h coinciding with high algal cell densities. Toxin burdens were assessed within different parts of the shellfish tissue, with the highest levels quantified in the mantle during the first 18 h period but shifting towards the gut thereafter. A comparison of toxin profile data evidenced the conversion of GTX1,4 in the source algae to the less potent GTX2,3 in the shellfish tissue. Overall, the study illustrated the temporal variability in Perna viridis toxin concentrations during a modelled algal bloom event, and the accumulation of toxin from the water even after toxic algae were removed.

ACS Style

John Kristoffer Andres; Aletta T. Yñiguez; Jennifer Mary Maister; Andrew D. Turner; Dave Eldon B. Olano; Jenelyn Mendoza; Lilibeth Salvador-Reyes; Rhodora V. Azanza. Paralytic Shellfish Toxin Uptake, Assimilation, Depuration, and Transformation in the Southeast Asian Green-Lipped Mussel (Perna viridis). Toxins 2019, 11, 468 .

AMA Style

John Kristoffer Andres, Aletta T. Yñiguez, Jennifer Mary Maister, Andrew D. Turner, Dave Eldon B. Olano, Jenelyn Mendoza, Lilibeth Salvador-Reyes, Rhodora V. Azanza. Paralytic Shellfish Toxin Uptake, Assimilation, Depuration, and Transformation in the Southeast Asian Green-Lipped Mussel (Perna viridis). Toxins. 2019; 11 (8):468.

Chicago/Turabian Style

John Kristoffer Andres; Aletta T. Yñiguez; Jennifer Mary Maister; Andrew D. Turner; Dave Eldon B. Olano; Jenelyn Mendoza; Lilibeth Salvador-Reyes; Rhodora V. Azanza. 2019. "Paralytic Shellfish Toxin Uptake, Assimilation, Depuration, and Transformation in the Southeast Asian Green-Lipped Mussel (Perna viridis)." Toxins 11, no. 8: 468.

Journal article
Published: 15 July 2019 in Journal of Peptide Science
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Two conomarphins were purified as the major component of the venom of Conus eburneus. Conomarphins Eb1 and Eb2 showed biological activity in the mollusk Pomacea padulosa, causing sluggishness and retraction of siphon, foot, and cephalic tentacles. To further probe the effects of conserved amino acids and posttranslational modifications in conomarphins, we prepared four synthetic analogues: conomarphin Eb1 Hyp10Pro, Hyp10Ala, d-Phe13Ala, and l-Phe13 variants. Structure-activity relationship analysis indicated that d-Phe13 is critical to the biological activity of conomarphins. In contrast, amino acid changes at position 10 and removal of posttranslational modification in Hyp10Pro can be tolerated. The high expression level and observed mollusk activity of conomarphins may suggest their potential role as defensive arsenal of Conoidean snails against other predatory gastropods.

ACS Style

Charmaine B. Mendoza; Dan Jethro M. Masacupan; Dessa Camille R. Batoctoy; Eizadora Yu; Arturo O. Lluisma; Lilibeth A. Salvador‐Reyes. Conomarphins cause paralysis in mollusk: Critical and tunable structural elements for bioactivity. Journal of Peptide Science 2019, 25, e3179 .

AMA Style

Charmaine B. Mendoza, Dan Jethro M. Masacupan, Dessa Camille R. Batoctoy, Eizadora Yu, Arturo O. Lluisma, Lilibeth A. Salvador‐Reyes. Conomarphins cause paralysis in mollusk: Critical and tunable structural elements for bioactivity. Journal of Peptide Science. 2019; 25 (7):e3179.

Chicago/Turabian Style

Charmaine B. Mendoza; Dan Jethro M. Masacupan; Dessa Camille R. Batoctoy; Eizadora Yu; Arturo O. Lluisma; Lilibeth A. Salvador‐Reyes. 2019. "Conomarphins cause paralysis in mollusk: Critical and tunable structural elements for bioactivity." Journal of Peptide Science 25, no. 7: e3179.

Journal article
Published: 20 December 2018 in Aquaculture
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Open-sea mariculture of the Philippine blue sponge Xestospongia sp. was established as a route for the production of the biomedically-important renieramycins. We assessed the effects of harvesting regime, culture period or periodicity, sponge translocation and farming methods to sponge survival, sponge growth, chemistry and bioactivity of sponge extracts. During the 12-month culture, sponge growth, renieramycin M content and antiproliferative activity of sponge extracts showed significant differences, depending on the culture period and location. Growth and renieramycin biosynthesis were minimally affected by temperature and may be driven by thermal-independent processes in the coral reef. Multiple harvesting of Xestospongia sp. was also favorable to growth and consequently, provided higher biomass and renieramycin M yields.

ACS Style

Viviene Santiago; Geminne G. Manzano; Clairecynth C. Yu; Porfirio M. Aliño; Lilibeth A. Salvador-Reyes. Mariculture potential of renieramycin-producing Philippine blue sponge Xestospongia sp. (Porifera: Haplosclerida). Aquaculture 2018, 502, 356 -364.

AMA Style

Viviene Santiago, Geminne G. Manzano, Clairecynth C. Yu, Porfirio M. Aliño, Lilibeth A. Salvador-Reyes. Mariculture potential of renieramycin-producing Philippine blue sponge Xestospongia sp. (Porifera: Haplosclerida). Aquaculture. 2018; 502 ():356-364.

Chicago/Turabian Style

Viviene Santiago; Geminne G. Manzano; Clairecynth C. Yu; Porfirio M. Aliño; Lilibeth A. Salvador-Reyes. 2018. "Mariculture potential of renieramycin-producing Philippine blue sponge Xestospongia sp. (Porifera: Haplosclerida)." Aquaculture 502, no. : 356-364.

Journal article
Published: 16 September 2017 in Marine Drugs
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Kempopeptin C, a novel chlorinated analogue of kempopeptin B, was discovered from a marine cyanobacterium collected from Kemp Channel in Florida. The structure was elucidated using NMR spectroscopy and mass spectrometry (MS). The presence of the basic Lys residue adjacent to the N-terminus of the 3-amino-6-hydroxy-2-piperidone (Ahp) moiety contributed to its selectivity towards trypsin and related proteases. The antiproteolytic activity of kempopeptin C was evaluated against trypsin, plasmin and matriptase and found to inhibit these enzymes with IC50 values of 0.19, 0.36 and 0.28 μM, respectively. Due to the significance of these proteases in cancer progression and metastasis, as well as their functional redundancy with respect to targeting overlapping substrates, we examined the effect of kempopeptin C on the downstream cellular substrates of matriptase: CDCP1 and desmoglein-2 (Dsg-2). Kempopeptin C was shown to inhibit the cleavage of both substrates in vitro. Additionally, kempopeptin C reduced the cleavage of CDCP1 in MDA-MB-231 cells up to 10 µM. The functional relevance of targeting matriptase and related proteases was investigated by assessing the effect of kempopeptin C on the migration of breast cancer cells. Kempopeptin C inhibited the migration of the invasive MDA-MB-231 cells by 37 and 60% at 10 and 20 µM, respectively.

ACS Style

Fatma Al-Awadhi; Lilibeth A. Salvador; Brian K. Law; Valerie J. Paul; Hendrik Luesch. Kempopeptin C, a Novel Marine-Derived Serine Protease Inhibitor Targeting Invasive Breast Cancer. Marine Drugs 2017, 15, 290 .

AMA Style

Fatma Al-Awadhi, Lilibeth A. Salvador, Brian K. Law, Valerie J. Paul, Hendrik Luesch. Kempopeptin C, a Novel Marine-Derived Serine Protease Inhibitor Targeting Invasive Breast Cancer. Marine Drugs. 2017; 15 (9):290.

Chicago/Turabian Style

Fatma Al-Awadhi; Lilibeth A. Salvador; Brian K. Law; Valerie J. Paul; Hendrik Luesch. 2017. "Kempopeptin C, a Novel Marine-Derived Serine Protease Inhibitor Targeting Invasive Breast Cancer." Marine Drugs 15, no. 9: 290.