Biodiversitas Alga Makro Di Lagun Pulau Pasige, Kecamatan Tagulandang, Kabupaten Sitaro

Alga makro sebagai salah satu sumberdaya yang ada di perairan Indonesia dimanfaatkan sebagai bahan baku makanan misalnya Gracilaria, Euchema dan Kappaphycus, disamping itu juga untuk kebutuhan farmasi, kosmetik, kertas dan cat, alga bernilai ekonomis penting dan memiliki tingkat kegunaan yang tinggi karena komoditas alga laut dapat bermanfaat baik bagi manusia maupun lingkungan perairan sekitarnya. Penelitian ini bertujuan untuk mengetahui jenis-jenis alga makro yang ada di perairan Pulau Pasige, Kecamatan Tagulandang, Kabupaten Sitaro dengan mengidentifikasi jenis-jenis alga makro yang ditemukan. Dari hasil penelitian ini ditemukan ada 9 jenis alga hijau Halimeda macroloba, Halimeda opuntia, Halimeda discoidea, Halimeda incrassata, Caulerpa lentillifera,Caulerpa racemosa, Boergesenia forbesii, Dictyospheria cavernosa, Boodlea coacta 10 alga merah Gracilaria blodgetti, Gracilaria edulis, Laurencia papilosa, Amphiroa fragilisima, Gelidiopsis intricata, Gracilaria verucosa, Acanthopeltis sp, Hypnea sp, Amansia glomerata, Euchema denticulatum dan 2 alga coklat Padina minor, Turbinaria ornata.

High Mannose-binding Lectin with Preference for the Cluster of α1–2-Mannose from the Green Alga Boodlea coacta Is a Potent Entry Inhibitor of HIV-1 and Influenza Viruses

The complete amino acid sequence of a lectin from the green alga Boodlea coacta (BCA), which was determined by a combination of Edman degradation of its peptide fragments and cDNA cloning, revealed the following: 1) B. coacta used a noncanonical genetic code (where TAA and TAG codons encode glutamine rather than a translation termination), and 2) BCA consisted of three internal tandem-repeated domains, each of which contains the sequence motif similar to the carbohydrate-binding site of Galanthus nivalis agglutinin-related lectins. Carbohydrate binding specificity of BCA was examined by a centrifugal ultrafiltration-HPLC assay using 42 pyridylaminated oligosaccharides. BCA bound to high mannose-type N-glycans but not to the complex-type, hybrid-type core structure of N-glycans or oligosaccharides from glycolipids. This lectin had exclusive specificity for α1–2-linked mannose at the nonreducing terminus. The binding activity was enhanced as the number of terminal α1–2-linked mannose substitutions increased. Mannobiose, mannotriose, and mannopentaose were incapable of binding to BCA. Thus, BCA preferentially recognized the nonreducing terminal α1–2-mannose cluster as a primary target. As predicted from carbohydrate-binding propensity, this lectin inhibited the HIV-1 entry into the host cells at a half-maximal effective concentration of 8.2 nm. A high association constant (3.71 × 108m−1) of BCA with the HIV envelope glycoprotein gp120 was demonstrated by surface plasmon resonance analysis. Moreover, BCA showed the potent anti-influenza activity by directly binding to viral envelope hemagglutinin against various strains, including a clinical isolate of pandemic H1N1-2009 virus, revealing its potential as an antiviral reagent.