Structure and assembly of the cortical microtubule cytoskeleton in the green alga,Boodlea coacta

PROTOPLASMA ◽  
1995 ◽  
Vol 189 (1-2) ◽  
pp. 113-122 ◽  
Author(s):  
S. Mizuta ◽  
T. Tsuji ◽  
T. Morinaga ◽  
S. Tsurumi
Keyword(s):  
Green Alga ◽  
Cortical Microtubule ◽  
Microtubule Cytoskeleton ◽  
Boodlea Coacta

scholarly journals 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

2011 ◽  
Vol 286 (22) ◽  
pp. 19446-19458 ◽  
Author(s):  
Yuichiro Sato ◽  
Makoto Hirayama ◽  
Kinjiro Morimoto ◽  
Naoki Yamamoto ◽  
Satomi Okuyama ◽  
...  
Keyword(s):  
Green Alga ◽  
Influenza Viruses ◽  
Viral Envelope ◽  
Host Cells ◽  
Carbohydrate Binding ◽  
Sequence Motif ◽  
High Association ◽  
High Mannose ◽  
Hiv 1 ◽  
Boodlea Coacta

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.

scholarly journals Author response: H+- and Na+- elicited rapid changes of the microtubule cytoskeleton in the biflagellated green alga Chlamydomonas

2017 ◽  
Author(s):  
Yi Liu ◽  
Mike Visetsouk ◽  
Michelle Mynlieff ◽  
Hongmin Qin ◽  
Karl F Lechtreck ◽  
...  
Keyword(s):  
Green Alga ◽  
Author Response ◽  
Microtubule Cytoskeleton ◽  
Rapid Changes
Sign in / Sign up

Export Citation Format

Share Document