scholarly journals A S‐Layer Protein of Bacillus anthracis as a Building Block for Functional Protein Arrays by In Vitro Self‐Assembly

Small ◽  
2015 ◽  
Vol 11 (43) ◽  
pp. 5826-5832 ◽  
Author(s):  
Xu‐Ying Wang ◽  
Dian‐Bing Wang ◽  
Zhi‐Ping Zhang ◽  
Li‐Jun Bi ◽  
Ji‐Bin Zhang ◽  
...  
Keyword(s):  
Bacillus Anthracis ◽  
Self Assembly ◽  
Building Block ◽  
Functional Protein ◽  
Protein Arrays

scholarly journals Bacillus anthracis SlaQ Promotes S-Layer Protein Assembly

2015 ◽  
Vol 197 (19) ◽  
pp. 3216-3227 ◽  
Author(s):  
Sao-Mai Nguyen-Mau ◽  
So-Young Oh ◽  
Daphne I. Schneewind ◽  
Dominique Missiakas ◽  
Olaf Schneewind
Keyword(s):  
Bacillus Anthracis ◽  
Self Assembly ◽  
Protein Assembly ◽  
Crystalline Lattice ◽  
Cell Wall Polysaccharide ◽  
Cytoplasmic Protein ◽  
Content Type ◽  
Bacterial Surface

ABSTRACTBacillus anthracisvegetative forms assemble an S-layer comprised of two S-layer proteins, Sap and EA1. A hallmark of S-layer proteins are their C-terminal crystallization domains, which assemble into a crystalline lattice once these polypeptides are deposited on the bacterial surface via association between their N-terminal S-layer homology domains and the secondary cell wall polysaccharide. Here we show thatslaQ, encoding a small cytoplasmic protein conserved among pathogenic bacilli elaborating S-layers, is required for the efficient secretion and assembly of Sap and EA1. S-layer protein precursors cosediment with SlaQ, and SlaQ appears to facilitate Sap assembly. Purified SlaQ polymerizes and when mixed with purified Sap promotes thein vitroformation of tubular S-layer structures. A model is discussed whereby SlaQ, in conjunction with S-layer secretion factors SecA2 and SlaP, promotes localized secretion and S-layer assembly inB. anthracis.IMPORTANCES-layer proteins are endowed with the propensity for self-assembly into crystalline arrays. Factors promoting S-layer protein assembly have heretofore not been reported. We identifiedBacillus anthracisSlaQ, a small cytoplasmic protein that facilitates S-layer protein assemblyin vivoandin vitro.

scholarly journals In vitro self-assembly of tailorable nanotubes from a simple protein building block

2008 ◽  
Vol 105 (10) ◽  
pp. 3733-3738 ◽  
Author(s):  
E. R. Ballister ◽  
A. H. Lai ◽  
R. N. Zuckermann ◽  
Y. Cheng ◽  
J. D. Mougous
Keyword(s):  
Self Assembly ◽  
Building Block

Self-assembly of vesicle nanoarrays on Si: A potential route to high-density functional protein arrays

2007 ◽  
Vol 90 (3) ◽  
pp. 033901 ◽  
Author(s):  
C. S. Ramanujan ◽  
K. Sumitomo ◽  
M. R. R. de Planque ◽  
H. Hibino ◽  
K. Torimitsu ◽  
...  
Keyword(s):  
Self Assembly ◽  
Density Functional ◽  
High Density ◽  
Functional Protein ◽  
Protein Arrays

In vitro and in vivo polysaccharides assembly: ultrastructural and cytochemical study of growing plant cell wall components.

1978 ◽  
Vol 36 (2) ◽  
pp. 434-435
Author(s):  
D. Reis ◽  
B. Vian ◽  
J. C. Roland
Keyword(s):  
Cell Wall ◽  
Self Assembly ◽  
Plant Cell Wall ◽  
Higher Plants ◽  
Three Dimensional ◽  
Cytochemical Study ◽  
Wall Components

Wall morphogenesis in higher plants is a problem still open to controversy. Until now the possibility of a transmembrane control and the involvement of microtubules were mostly envisaged. Self-assembly processes have been observed in the case of walls of Chlamydomonas and bacteria. Spontaneous gelling interactions between xanthan and galactomannan from Ceratonia have been analyzed very recently. The present work provides indications that some processes of spontaneous aggregation could occur in higher plants during the formation and expansion of cell wall.Observations were performed on hypocotyl of mung bean (Phaseolus aureus) for which growth characteristics and wall composition have been previously defined.In situ, the walls of actively growing cells (primary walls) show an ordered three-dimensional organization (fig. 1). The wall is typically polylamellate with multifibrillar layers alternately transverse and longitudinal. Between these layers intermediate strata exist in which the orientation of microfibrils progressively rotates. Thus a progressive change in the morphogenetic activity occurs.

Programmable in vitro Co-Encapsidation of Guest Proteins Inside Protein Nanocages

2018 ◽  
Author(s):  
Noor H. Dashti ◽  
Rufika S. Abidin ◽  
Frank Sainsbury
Keyword(s):  
Self Assembly ◽  
Mammalian Cells ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Super Resolution ◽  
Cell Engineering ◽  
Particle Analysis ◽  
Protein Cages

Bioinspired self-sorting and self-assembling systems using engineered versions of natural protein cages have been developed for biocatalysis and therapeutic delivery. The packaging and intracellular delivery of guest proteins is of particular interest for both <i>in vitro</i> and <i>in vivo</i> cell engineering. However, there is a lack of platforms in bionanotechnology that combine programmable guest protein encapsidation with efficient intracellular uptake. We report a minimal peptide anchor for <i>in vivo</i> self-sorting of cargo-linked capsomeres of the Murine polyomavirus (MPyV) major coat protein that enables controlled encapsidation of guest proteins by <i>in vitro</i> self-assembly. Using Förster resonance energy transfer (FRET) we demonstrate the flexibility in this system to support co-encapsidation of multiple proteins. Complementing these ensemble measurements with single particle analysis by super-resolution microscopy shows that the stochastic nature of co-encapsidation is an overriding principle. This has implications for the design and deployment of both native and engineered self-sorting encapsulation systems and for the assembly of infectious virions. Taking advantage of the encoded affinity for sialic acids ubiquitously displayed on the surface of mammalian cells, we demonstrate the ability of self-assembled MPyV virus-like particles to mediate efficient delivery of guest proteins to the cytosol of primary human cells. This platform for programmable co-encapsidation and efficient cytosolic delivery of complementary biomolecules therefore has enormous potential in cell engineering.

scholarly journals Development of In Situ Self-Assembly Nanoparticles to Encapsulate Lopinavir and Ritonavir for Long-Acting Subcutaneous Injection

Pharmaceutics ◽  
2021 ◽  
Vol 13 (6) ◽  
pp. 904
Author(s):  
Irin Tanaudommongkon ◽  
Asama Tanaudommongkon ◽  
Xiaowei Dong
Keyword(s):  
Sustained Release ◽  
Trough Concentration ◽  
Self Assembly ◽  
Subcutaneous Injection ◽  
Drug Loading ◽  
Entrapment Efficiency ◽  
Long Acting

Most antiretroviral medications for human immunodeficiency virus treatment and prevention require high levels of patient adherence, such that medications need to be administered daily without missing doses. Here, a long-acting subcutaneous injection of lopinavir (LPV) in combination with ritonavir (RTV) using in situ self-assembly nanoparticles (ISNPs) was developed to potentially overcome adherence barriers. The ISNP approach can improve the pharmacokinetic profiles of the drugs. The ISNPs were characterized in terms of particle size, drug entrapment efficiency, drug loading, in vitro release study, and in vivo pharmacokinetic study. LPV/RTV ISNPs were 167.8 nm in size, with a polydispersity index of less than 0.35. The entrapment efficiency was over 98% for both LPV and RTV, with drug loadings of 25% LPV and 6.3% RTV. A slow release rate of LPV was observed at about 20% on day 5, followed by a sustained release beyond 14 days. RTV released faster than LPV in the first 5 days and slower than LPV thereafter. LPV trough concentration remained above 160 ng/mL and RTV trough concentration was above 50 ng/mL after 6 days with one subcutaneous injection. Overall, the ISNP-based LPV/RTV injection showed sustained release profiles in both in vitro and in vivo studies.

Design, Synthesis, and In Vitro Evaluation of Tubulin‐targeting Dibenzothiazines with Antiproliferative Activity as Novel Heterocycle Building Block

ChemMedChem ◽  
2021 ◽  
Author(s):  
Walter Damián Guerra ◽  
Daniel Lucena-Agell ◽  
Rafael Hortigüela ◽  
Roberto Arturo Rossi ◽  
J. Fernando Díaz ◽  
...  
Keyword(s):  
Antiproliferative Activity ◽  
Building Block ◽  
Design Synthesis ◽  
In Vitro Evaluation

Engineering two mutants of cDNA-encoding G2 subunit of soybean glycinin capable of self-assembly in vitro and rich in methionine

Biologia ◽  
2007 ◽  
Vol 62 (4) ◽  
Author(s):  
Reda Sammour
Keyword(s):  
Amino Acid ◽  
Self Assembly ◽  
Seed Quality ◽  
Amino Acid Residues ◽  
Methionine Residues

AbstractThe main goal of this work was to make the cDNA-encoding subunit G2 of soybean glycinin, capable of self-assembly in vitro and rich in methionine residues. Two mutants (pSP65/G4SacG2 and pSP65/G4SacG2HG4) were therefore constructed. The constructed mutants were successfully assembled in vitro into oligomers similar to those occurred in the seed. The successful self-assembly was due to the introduction of Sac fragment of Gy4 (the codons of the first 21 amino acid residues), which reported to be the key element in self-assembly into trimers. The mutant pSP65/G4SacG2HG4 included the acidic chain of Gy4 (HG4), which was previously molecularly modified to have three methionine residues. This mutant will be useful in the efforts to improve the seed quality.

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