Liquid-crystalline ordering in bacterial cellulose produced by Gluconacetobaсter hansenii on glucose-containing media.

This research is dedicated to the studies of the microscale morphology of bacterial cellulose (BC) obtained by means of static cultivation of Gluconacetobacter hansenii GH-1/2008. We found that the microscale morphology depended on the BC production rate that was varied by using different glucose concentrations in the cultivation medium. It was revealed that at higher production rates, BC fibrils were aligned in a liquid-crystalline-like (LC-like) order. The observed helical alignment was always left-handed. The half-periods of the helix varied from 50 µm to 150 µm depending on the cultivation conditions. The mechanical and water absorption properties of the obtained BC pellicles were measured. The former correlated mainly with the density of the samples; the latter were the best for films with layered structure, where the BC had segregated into fleece sheets separated by gaps with low density of fibrils.

Structural organization of bacterial cellulose: The origin of anisotropy and layered structures.

In this paper, we perform a systematic analysis of the structural organization of bacterial cellulose (BC). We report four types of organization of the BC mass, produced by Gluconacetobacter hansenii that occur depending on cultivation conditions. Two of those, particularly, plywood type one and layers of micro-sized tubes were observed and described for the first time. In spherical BC particles (pellets), we found the layered structure that had previously been reported for planar geometry only. We suggest a model explaining why layers form in BC films and attempt to reveal the impact of different factors on the BC microscale morphology. We assume that the main factor that has direct impact on the type of structure formed is the rate of BC mass accumulation.

Chitosan coatings with enhanced biostability in vivo.

In this article, we study the stability of chitosan coatings applied on glutaraldehyde-stabilized bovine pericardium when exposed to biodegradation in vivo in the course of model subcutaneous tests on rats. The coatings were deposited from carbonic acid solutions, that is, H2 O saturated with CO2 at high pressure. Histological sections of treated pericardium samples demonstrated that the structure of pericardial connective tissues was not significantly altered by the coating application method. It was revealed that the dynamics of biodegradation depended on the total mass of chitosan applied as well as on the DDA of chitosan used. As long as the amount of chitosan did not exceed a certain threshold limit, no detectable degradation occurred within the time of the tests (12 weeks for the rat model). For higher chitosan amounts, we detected a ∼20% reduction of the mass after the in vivo exposition. The presumed mechanism of such behavior is discussed. © 2017 Wiley Periodicals, Inc. J Biomed Mater Res Part B: Appl Biomater, 106B: 270-277, 2018.

Structural organization of mRNA complexes with major core mRNP protein YB-1.

YB-1 is a universal major protein of cytoplasmic mRNPs, a member of the family of multifunctional cold shock domain proteins (CSD proteins). Depending on its amount on mRNA, YB-1 stimulates or inhibits mRNA translation. In this study, we have analyzed complexes formed in vitro at various YB-1 to mRNA ratios, including those typical for polysomal (translatable) and free (untranslatable) mRNPs. We have shown that at mRNA saturation with YB-1, this protein alone is sufficient to form mRNPs with the protein/RNA ratio and the sedimentation coefficient typical for natural mRNPs. These complexes are dynamic structures in which the protein can easily migrate from one mRNA molecule to another. Biochemical studies combined with atomic force microscopy and electron microscopy showed that mRNA-YB-1 complexes with a low YB-1/mRNA ratio typical for polysomal mRNPs are incompact; there, YB-1 binds to mRNA as a monomer with its both RNA-binding domains. At a high YB-1/mRNA ratio typical for untranslatable mRNPs, mRNA-bound YB-1 forms multimeric protein complexes where YB-1 binds to mRNA predominantly with its N-terminal part. A multimeric YB-1 comprises about twenty monomeric subunits; its molecular mass is about 700 kDa, and it packs a 600-700 nt mRNA segment on its surface.

AFM study of potato virus X disassembly induced by movement protein.

Recently we have reported that a selective binding of potato virus X (PVX)-coded movement protein (termed TGBp1 MP) to one end of a polar coat protein (CP) helix converted viral RNA into a translatable form and induced a linear destabilization of the whole helical particle. Here, the native PVX virions, RNase-treated (PVX(RNA-DEG)) helical particles lacking intact RNA and their complexes with TGBp1 (TGBp1-PVX and TGBp1-PVX(RNA-DEG)), were examined by atomic force microscopy (AFM). When complexes of the TGBp1 MP with PVX were examined by means of AFM in liquid, no structural reorganization of PVX particles was observed. By contrast, the products of TGBp1-dependent PVX degradation termed "beads-on-string" were formed under conditions of AFM in air. The AFM images of PVX(RNA-DEG) were indistinguishable from images of native PVX particles; however, the TGBp1-dependent disassembly of the CP-helix was triggered when the TGBp1-PVX(RNA-DEG) complexes were examined by AFM, regardless of the conditions used (in air or in liquid). Our data supported the idea that binding of TGBp1 to one end of the PVX CP-helix induced linear destabilization of the whole helical particle, which may lead to its disassembly under conditions of AFM.

Microbial surfaces investigated using atomic force microscopy.

This paper is dedicated to atomic force microscopy (AFM) as a progressive tool for imaging bacterial surfaces and probing their properties. The description of the technique is complemented by the explanation of the method's artifacts typical, in particular, for the imaging of bacterial cells. Sample preparation techniques are summarized in a separate section. Special attention is paid to the differences in imaging of gram-positive and gram-negative bacteria. Probing of mechanical properties, including elastic modulus, fragility, and adhesion of the cell walls is emphasized. The advantages of AFM in the studies of real-time cellular dynamical processes are illustrated by the experiment with the germination of spores.