Modeling of the major gas vesicle protein, GvpA: From protein sequence to vesicle wall structure

Ezzeldin, Hussein; Klauda, Jeffery B.; Solares, Santiago D.

doi:10.1016/j.jsb.2012.04.015

Cited by 25 publications

(20 citation statements)

References 86 publications

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“…Accordingly, it might be hypothesized that these may represent another example of archaeal amyloids. This is supported by previous solid state NMR correlation spectroscopy data that provided evidence for an extended cross-␤ structure in gas vesicles from cyanobacteria (42,61).…”

Section: Discussionsupporting

confidence: 84%

The Tubular Sheaths Encasing Methanosaeta thermophila Filaments Are Functional Amyloids

Dueholm

Larsen

Finster

et al. 2015

Journal of Biological Chemistry

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Background: Many organisms benefit from functional amyloids. Archaea represent the only domain of life without any described functional amyloids. Results: Biophysical and recombinant techniques show that the sheaths of Methanosaeta thermophila PT are functional amyloid. Conclusion: Archaea produce functional amyloids. Significance: The amyloid nature explains many sheath properties that have puzzled researchers for years.

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Section: Discussionsupporting

confidence: 84%

The Tubular Sheaths Encasing Methanosaeta thermophila Filaments Are Functional Amyloids

Dueholm

Larsen

Finster

et al. 2015

Journal of Biological Chemistry

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“…The pfam741 family has been proposed to determine the curvature of the nanoparticle structure and/or to mediate the transition from cones to the cylindrical region. Spectroscopic and de novo modeling studies of GvpA have further suggested that this protein adopts a coil-α-β-β-α-coil fold with anti-parallel β-strands forming a hydrophobic surface on the internal face of the nanoparticles and a hydrophilic surface on the external side [ 75 , 76 , 77 ].…”

Section: Gas Vesicle Proteinsmentioning

confidence: 99%

Gas Vesicle Nanoparticles for Antigen Display

DasSarma

2015

Vaccines

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Microorganisms like the halophilic archaeon Halobacterium sp. NRC-1 produce gas-filled buoyant organelles, which are easily purified as protein nanoparticles (called gas vesicles or GVNPs). GVNPs are non-toxic, exceptionally stable, bioengineerable, and self-adjuvanting. A large gene cluster encoding more than a dozen proteins has been implicated in their biogenesis. One protein, GvpC, found on the exterior surface of the nanoparticles, can accommodate insertions near the C-terminal region and results in GVNPs displaying the inserted sequences on the surface of the nanoparticles. Here, we review the current state of knowledge on GVNP structure and biogenesis as well as available studies on immunogenicity of pathogenic viral, bacterial, and eukaryotic proteins and peptides displayed on the nanoparticles. Recent improvements in genetic tools for bioengineering of GVNPs are discussed, along with future opportunities and challenges for development of vaccines and other applications.

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“…A 3D model was derived from a high-performance de novo modelling of mcGvpA [ 63 ], and the model was confirmed for the almost identical GvpA of Hbt. salinarum NRC-1 [ 65 ]. The hydrophobic β-sheet portion most likely faces the gas phase and prevents the precipitation of water molecules entering the gas-filled core.…”

Section: Gas Vesicle Wall and Mutations Affecting The Shapementioning

confidence: 99%

Haloarchaea and the Formation of Gas Vesicles

Pfeifer

2015

Life

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Halophilic Archaea (Haloarchaea) thrive in salterns containing sodium chloride concentrations up to saturation. Many Haloarchaea possess genes encoding gas vesicles, but only a few species, such as Halobacterium salinarum and Haloferax mediterranei, produce these gas-filled, proteinaceous nanocompartments. Gas vesicles increase the buoyancy of cells and enable them to migrate vertically in the water body to regions with optimal conditions. Their synthesis depends on environmental factors, such as light, oxygen supply, temperature and salt concentration. Fourteen gas vesicle protein (gvp) genes are involved in their formation, and regulation of gvp gene expression occurs at the level of transcription, including the two regulatory proteins, GvpD and GvpE, but also at the level of translation. The gas vesicle wall is solely formed of proteins with the two major components, GvpA and GvpC, and seven additional accessory proteins are also involved. Except for GvpI and GvpH, all of these are required to form the gas permeable wall. The applications of gas vesicles include their use as an antigen presenter for viral or pathogen proteins, but also as a stable ultrasonic reporter for biomedical purposes.

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Modeling of the major gas vesicle protein, GvpA: From protein sequence to vesicle wall structure

Cited by 25 publications

References 86 publications

The Tubular Sheaths Encasing Methanosaeta thermophila Filaments Are Functional Amyloids

The Tubular Sheaths Encasing Methanosaeta thermophila Filaments Are Functional Amyloids

Gas Vesicle Nanoparticles for Antigen Display

Haloarchaea and the Formation of Gas Vesicles

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