Notting Hill, Australia
Notting Hill, Australia

Biota was an Australian antiviral drug development company listed on the Australian Stock Exchange . In 1989 Biota discovered the drug Zanamivir, which acts as a neuraminidase inhibitor for the treatment and prevention of influenza. This drug is licensed to GlaxoSmithKline and marketed as Relenza. In November 2012, Biota Holdings Limited merged with American company Nabi Biopharmaceuticals to form Biota Pharmaceuticals.The combined company has its headquarters in the U.S. and is now listed on the NASDAQ under the abbreviated code BOTA. Wikipedia.


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Porter K.,Biota Holdings | Tang S.-L.,Academia Sinica, Taiwan | Chen C.-P.,Academia Sinica, Taiwan | Chiang P.-W.,Academia Sinica, Taiwan | And 2 more authors.
Archaea | Year: 2013

Halovirus PH1 infects Haloarcula hispanica and was isolated from an Australian salt lake. The burst size in single-step growth conditions was 50-100 PFU/cell, but cell density did not decrease until well after the rise (4-6 hr p.i.), indicating that the virus could exit without cell lysis. Virions were round, 51 nm in diameter, displayed a layered capsid structure, and were sensitive to chloroform and lowered salt concentration. The genome is linear dsDNA, 28,064 bp in length, with 337 bp terminal repeats and terminal proteins, and could transfect haloarchaeal species belonging to five different genera. The genome is predicted to carry 49 ORFs, including those for structural proteins, several of which were identified by mass spectroscopy. The close similarity of PH1 to SH1 (74% nucleotide identity) allowed a detailed description and analysis of the differences (divergent regions) between the two genomes, including the detection of repeat-mediated deletions. The relationship of SH1-like and pleolipoviruses to previously described genomic loci of virus and plasmid-related elements (ViPREs) of haloarchaea revealed an extensive level of recombination between the known haloviruses. PH1 is a member of the same virus group as SH1 and HHIV-2, and we propose the name halosphaerovirus to accommodate these viruses. © 2013 Kate Porter et al.


Carr J.M.,CSIRO | Duggan P.J.,CSIRO | Humphrey D.G.,CSIRO | Humphrey D.G.,ArchWood Protection Aust Pty Ltd | And 3 more authors.
Australian Journal of Chemistry | Year: 2010

In continuation of a program aimed at developing a boron-based, high performing and environmentally benign wood preservative suitable for outdoor use, three lipophilic tetra-n-butylammonium spiroborates, tetra-n-butylammonium bis[naphthalene-2,3-diolato(2-)-O,O′]borate 4, tetra-n-butylammonium bis[2,2′-biphenolato(2-)-O,O′]borate 5 and tetra-n-butylammonium bis[3-hydroxy-2-naphthoato(2-)-O,O′]borate 6 were prepared and tested. The higher molecular weight and lipophilicity of these borates compared with related borates previously examined correlates, in the case of 5 and 6, with significantly enhanced leach resistance while termiticidal activity has been maintained. The racemic spiroborate derived from 2,2′-biphenol 5, in particular, appears to be close to an optimum balance between ease of synthesis, solubility, hydrolytic stability and termiticidal activity. © 2010 CSIRO.


Doak B.C.,Monash University | Morton C.J.,Biota Holdings | Simpson J.S.,Monash University | Scanlon M.J.,Monash University
Australian Journal of Chemistry | Year: 2013

The design of a suitable library is an essential prerequisite to establish a fragment-based screening capability. Several pharmaceutical companies have described their approaches to establishing fragment libraries; however there are few detailed reports of both design and analysis of performance for a fragment library maintained in an academic setting. Here we report our efforts towards the design of a fragment library for nuclear magnetic resonance spectroscopy-based screening, demonstrate the performance of the library through analysis of 14 screens, and present a comparison to previously reported fragment libraries. © CSIRO 2013.


McMahon R.M.,University of Queensland | Coincon M.,University of Queensland | Coincon M.,University of Stockholm | Tay S.,University of Queensland | And 6 more authors.
Acta Crystallographica Section D: Biological Crystallography | Year: 2015

Pseudomonas aeruginosa is an opportunistic human pathogen for which new antimicrobial drug options are urgently sought. P. aeruginosa disulfide-bond protein A1 (PaDsbA1) plays a pivotal role in catalyzing the oxidative folding of multiple virulence proteins and as such holds great promise as a drug target. As part of a fragment-based lead discovery approach to PaDsbA1 inhibitor development, the identification of a crystal form of PaDsbA1 that was more suitable for fragment-soaking experiments was sought. A previously identified crystallization condition for this protein was unsuitable, as in this crystal form of PaDsbA1 the active-site surface loops are engaged in the crystal packing, occluding access to the target site. A single residue involved in crystal-packing interactions was substituted with an amino acid commonly found at this position in closely related enzymes, and this variant was successfully used to generate a new crystal form of PaDsbA1 in which the active-site surface is more accessible for soaking experiments. The PaDsbA1 variant displays identical redox character and in vitro activity to wild-type PaDsbA1 and is structurally highly similar. Two crystal structures of the PaDsbA1 variant were determined in complex with small molecules bound to the protein active site. These small molecules (MES, glycerol and ethylene glycol) were derived from the crystallization or cryoprotectant solutions and provide a proof of principle that the reported crystal form will be amenable to co-crystallization and soaking with small molecules designed to target the protein active-site surface. © 2015 International Union of Crystallography.


Trademark
Biota Pharmaceuticals Inc. and Biota Holdings | Date: 2014-11-18

pharmaceutical preparations for use as anti-infectives, namely, antivirals for use in the treatment of infectious diseases and conditions; drugs for use as anti-infectives, namely, antivirals for use in the treatment of infectious diseases and conditions, and diagnostic preparations for medical purposes. Pharmaceutical and chemical research.


PubMed | University of Queensland, Monash Institute of Pharmaceutical Sciences and Biota Holdings
Type: Journal Article | Journal: Acta crystallographica. Section D, Biological crystallography | Year: 2015

Pseudomonas aeruginosa is an opportunistic human pathogen for which new antimicrobial drug options are urgently sought. P. aeruginosa disulfide-bond protein A1 (PaDsbA1) plays a pivotal role in catalyzing the oxidative folding of multiple virulence proteins and as such holds great promise as a drug target. As part of a fragment-based lead discovery approach to PaDsbA1 inhibitor development, the identification of a crystal form of PaDsbA1 that was more suitable for fragment-soaking experiments was sought. A previously identified crystallization condition for this protein was unsuitable, as in this crystal form of PaDsbA1 the active-site surface loops are engaged in the crystal packing, occluding access to the target site. A single residue involved in crystal-packing interactions was substituted with an amino acid commonly found at this position in closely related enzymes, and this variant was successfully used to generate a new crystal form of PaDsbA1 in which the active-site surface is more accessible for soaking experiments. The PaDsbA1 variant displays identical redox character and in vitro activity to wild-type PaDsbA1 and is structurally highly similar. Two crystal structures of the PaDsbA1 variant were determined in complex with small molecules bound to the protein active site. These small molecules (MES, glycerol and ethylene glycol) were derived from the crystallization or cryoprotectant solutions and provide a proof of principle that the reported crystal form will be amenable to co-crystallization and soaking with small molecules designed to target the protein active-site surface.


Oh D.,5 9 Waterman Terrace | Porter K.,Biota Holdings | Russ B.,University of Melbourne | Burns D.,148 Monaro Cres | Dyall-Smith M.,Max Planck Institute of Biochemistry
Extremophiles | Year: 2010

Haloquadratum walsbyi is frequently a dominant member of the microbial communities in hypersaline waters. 16S rRNA gene sequences indicate that divergence within this species is very low but relatively few sites have been examined, particularly in the southern hemisphere. The diversity of Haloquadratum was examined in three coastal, but geographically distant saltern crystallizer ponds in Australia, using both culture-independent and culture-dependent methods. Two 97%-OTU, comprising Haloquadratum- and Halorubrum-related sequences, were shared by all three sites, with the former OTU representing about 40% of the sequences recovered at each site. Sequences 99.5% identical to that of Hqr. walsbyi C23T were present at all three sites and, overall, 98% of the Haloquadratum-related sequences displayed ≤2% divergence from that of the type strain. While haloarchaeal diversity at each site was relatively low (9-16 OTUs), seven phylogroups (clones and/or isolates) and 4 different clones showed ≤90% sequence identity to classified taxa, and appear to represent novel genera. Six of these branched together in phylogenetic tree reconstructions, forming a clade (MSP8-clade) whose members were only distantly related to classified taxa. Such sequences have only rarely been previously detected but were found at all three Australian crystallizers. © 2009 The Author(s).


Trademark
Biota Holdings | Date: 2012-10-23

Vaccines, pharmaceutical preparations, drugs and diagnostic preparations for clinical and medical use as anti-infectives, namely, antivirals and antibacterials for use in the treatment or diagnosis of infectious diseases and conditions.


News Article | July 16, 2012
Site: www.eweek.com

IBM technology is helping fight the common cold. Researchers in Melbourne, Australia, are now simulating in 3D the motion of the complete human rhinovirus (HRV), the most frequent cause of the common cold, using Australia€™s fastest supercomputer, an IBM Blue Gene/Q.A new antiviral drug to treat rhinovirus infections is being developed by Melbourne company Biota Holdings Ltd., targeted for those with these existing conditions where the common cold is a serious threat to their health and could prove fatal. In conjunction with researchers at the IBM Research Collaboratory for Life Sciences€“Melbourne, scientists from St. Vincent€™s Institute of Medical Research and the University of Melbourne are using information on how the new drug works to create a 3D simulation of the complete rhinovirus on IBM supercomputing technology.To help pave the way for new drug development, researchers are working to build a fully atomistic, three-dimensional simulation of HRV. According to IBM, these calculations are the first to include not only the 3 million-plus atoms of the rhinovirus capsid€”or outer shell€”and their aqueous environment, but also the virus€™ RNA genome, that packet of genetic information necessary for the virus to replicate. A new antiviral drug to treat rhinovirus infections is being developed by Melbourne company Biota Holdings Ltd., targeted for those with conditions where the common cold is a serious threat to their health and could prove fatal. Rhinovirus infection is linked to about 70 percent of all asthma exacerbations, with more than 50 percent of these patients requiring hospitalization. Furthermore, over 35 percent of patients with acute chronic obstructive pulmonary disease (COPD) are hospitalized each year due to respiratory viruses including rhinovirus. A team of researchers led by Professor Michael Parker from St. Vincent€™s Institute of Medical Research (SVI) and the University of Melbourne are now using information on how the new drug works to create a 3D simulation of the complete rhinovirus using Australia€™s fastest supercomputer. €œOur recently published work with Biota shows that the drug binds to the shell that surrounds the virus, called the capsid,€ Parker said in a statement. €œBut that work doesn€™t explain in precise detail how the drug and other similar acting compounds work.€ Professor Parker and his team are working on the newly installed IBM Blue Gene/Q at the University of Melbourne with computational biologists from IBM and the Victorian Life Sciences Computation Initiative (VLSCI). In production since July 1, 2012, the IBM Blue Gene/Q is the most powerful supercomputer dedicated to life sciences research in the Southern Hemisphere and currently ranked the fastest in Australia. €œThe IBM Blue Gene/Q will provide us with extraordinary 3D computer simulations of the whole virus in a time frame not even dreamt of before,€ Parker said. €œSupercomputer technology enables us to delve deeper in the mechanisms at play inside a human cell, particularly how drugs work at a molecular level. €œThis work offers exciting opportunities for speeding up the discovery and development of new antiviral treatments and hopefully will save many lives around the world,€ he said. Professor Parker said that previous efforts have only been able to focus on running smaller simulations on just parts of the virus. However, Professor James McCluskey, deputy vice chancellor for research at the University of Melbourne, said: €œThe work on rhinovirus is an example of how new approaches to treat disease will become possible with the capacity of the IBM Blue Gene Q, exactly how we hoped this extraordinary asset would be utilized by the Victorian research community in collaboration with IBM. €œThis is a terrific facility for Victorian life science researchers, further strengthening Victoria€™s reputation as a leading biotechnology centre,€ he said. John Wagner, Ph.D., manager of the IBM Research Collaboratory for Life Sciences-Melbourne, co-located at the VLSCI, said these types of simulations are the way of the future for drug discovery. €œThis is the way we do biology in the 21st Century,€ he said. The newly operational IBM Blue Gene/Q hosted by the University of Melbourne at the VLSCI is ranked 31st on the prestigious global TOP500 list . The TOP500 table nominates the 500 most powerful computer systems in the world. The VLSCI is an initiative of the Victorian Government in partnership with the University of Melbourne and the IBM Life Sciences Research Collaboratory, Melbourne.

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