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Rational design of potent sialidase-based inhibitors of influenza virus replication

Mark von Itzstein
Wen-Yang Wu
Charles R. Penn
Research03 Jun 1993
Nature

Volume: 363, P: 418-423
The war against influenza: discovery and development of sialidase inhibitors

The threat of an influenza pandemic has heightened the need for therapeutic strategies to combat this virus. This article provides a historical perspective on the discovery and development of two drugs that are at the forefront of our defences against influenza — the sialdiase inhibitors zanamivir and oseltamivir — highlighting the value of structure-based drug design in this process.

Mark von Itzstein
Reviews01 Dec 2007
Nature Reviews Drug Discovery

Volume: 6, P: 967-974
Neutralizing the pathological effects of extracellular histones with small polyanions

Histones, proteins that bind DNA, are toxic for pathogens outside cells but can also cause multi-organ damage as seen in sepsis. Here the authors develop small negatively charged molecules that can be used as histone antidotes, and show that they improve the phenotype in mouse models with histone-related pathologies.

Connor H. O’ Meara
Lucy A. Coupland
Christopher R. Parish
ResearchOpen Access16 Dec 2020
Nature Communications

Volume: 11, P: 1-17
Structure-guided discovery of potent and dual-acting human parainfluenza virus haemagglutinin–neuraminidase inhibitors

Human parainfluenza viruses (hPIVs) cause common respiratory diseases in children. Here the authors rationally design small molecules targeting the hPIV haemagglutinin–neuraminidase protein, and show that the compounds inhibit viral entry and exit from cultured cells.

Patrice Guillon
Larissa Dirr
Mark von Itzstein
Research20 Oct 2014
Nature Communications

Volume: 5, P: 1-11
Revisiting the role of histo-blood group antigens in rotavirus host-cell invasion

Histo-blood group antigens (HBGAs) have been proposed as essential cellular receptors for rotaviruses, which can cause severe diarrhoea in children. Here, the authors show that rotavirus strains display important variations in their ability to recognize different HBGAs.

Raphael Böhm
Fiona E. Fleming
Thomas Haselhorst
Research05 Jan 2015
Nature Communications

Volume: 6, P: 1-12
Sialic acid dependence in rotavirus host cell invasion

Thomas Haselhorst
Fiona E Fleming
Mark von Itzstein
Research21 Dec 2008
Nature Chemical Biology

Volume: 5, P: 91-93
Novel sialic acid derivatives lock open the 150-loop of an influenza A virus group-1 sialidase

The influenza virus life cycle relies on sialidases, which are classified as group-1 or group-2, depending on the flexibility of the '150-loop'. In this study, chemical compounds are developed, which lock open the '150-loop', selectively inhibiting the activity of group-1 sialidases.

Santosh Rudrawar
Jeffrey C. Dyason
Mark von Itzstein
ResearchOpen Access16 Nov 2010
Nature Communications

Volume: 1, P: 1-7
Production of α-L-iduronidase in maize for the potential treatment of a human lysosomal storage disease

The lysosomal storage disease mucopolysaccharidosis I is treated with recombinant α-L-iduronidase but production of the enzyme is expensive. In this study, α-L-iduronidase is compartmentalized within the endosperm of maize via a unique mRNA strategy yielding the active, correctly glycosylated protein.

Xu He
Thomas Haselhorst
Allison R. Kermode
Research18 Sept 2012
Nature Communications

Volume: 3, P: 1-9
Sialic acid catabolism drives intestinal inflammation and microbial dysbiosis in mice

Intestinal inflammation is often associated with a shift in microbiota composition but the mechanisms are unclear. Here the authors show that an increase in caecal sialidase activity occurring during intestinal inflammation promotes the expansion of Enterobacteriaceae, which can lead to exacerbated inflammatory response.

Yen-Lin Huang
Christophe Chassard
Thierry Hennet
ResearchOpen Access25 Aug 2015
Nature Communications

Volume: 6, P: 1-11
Ferrets exclusively synthesize Neu5Ac and express naturally humanized influenza A virus receptors

Ferrets constitute a useful model for influenza research because they are susceptible to human-adapted flu viruses. Here, the authors show that ferrets, like humans, lack a functional CMAH enzyme and synthesize a single type of sialic acid (Neu5Ac), resulting in naturally humanized influenza virus receptors.

Preston S.K. Ng
Raphael Böhm
Michael P. Jennings
ResearchOpen Access17 Dec 2014
Nature Communications

Volume: 5, P: 1-9
Functional and structural characterization of a heparanase

Structure and functional characterization of BpHep, a heparanase from the invasive pathogenic bacterium Burkholderia pseudomallei, defines its glycosaminoglycan recognition mechanism and its catalytic mechanism as an endo-acting glycoside hydrolase.

Lisa Bohlmann
Gregory D Tredwell
Mark von Itzstein
Research02 Nov 2015
Nature Chemical Biology

Volume: 11, P: 955-957
A dual drug regimen synergistically blocks human parainfluenza virus infection

Benjamin Bailly
Larissa Dirr
Mark von Itzstein
ResearchOpen Access07 Apr 2016
Scientific Reports

Volume: 6, P: 1-13
The impact of the butterfly effect on human parainfluenza virus haemagglutinin-neuraminidase inhibitor design

Larissa Dirr
Ibrahim M. El-Deeb
Mark von Itzstein
ResearchOpen Access03 Jul 2017
Scientific Reports

Volume: 7, P: 1-10
Heparanase interacting BCLAF1 to promote the development and drug resistance of ICC through the PERK/eIF2α pathway

Fengyan Yuan
Huiqin Zhou
Xing Yu
Research11 Mar 2024
Cancer Gene Therapy

Volume: 31, P: 904-916
Glycointeractions in bacterial pathogenesis

In this Review, Jennings and colleagues discuss interactions involving host and bacterial glycans that have a role in bacterial pathogenesis. They also highlight recent technological advances that have illuminated the glycoscience of microbial pathogenesis.

Jessica Poole
Christopher J. Day
Michael P. Jennings
Reviews19 Apr 2018
Nature Reviews Microbiology

Volume: 16, P: 440-452
Unravelling the Role of O-glycans in Influenza A Virus Infection

Juliane Mayr
Kam Lau
Thomas Haselhorst
ResearchOpen Access06 Nov 2018
Scientific Reports

Volume: 8, P: 1-12
Cyclization-blocked proguanil as a strategy to improve the antimalarial activity of atovaquone

Tina Skinner-Adams et al. show that proguanil and the cyclization-blocked analogue, tBuPG, have potent, anti-plasmodial activity in vitro. This study suggests that a cyclization-blocked proguanil may be a superior combination partner for bc1-inhibitors to suppress the survival of malarial parasites.

Tina S. Skinner-Adams
Gillian M. Fisher
Katherine T. Andrews
ResearchOpen Access03 May 2019
Communications Biology

Volume: 2, P: 1-14
Structural characterisation of high affinity Siglec-2 (CD22) ligands in complex with whole Burkitt’s lymphoma (BL) Daudi cells by NMR spectroscopy

Paul D. Madge
Andrea Maggioni
Thomas Haselhorst
ResearchOpen Access03 Nov 2016
Scientific Reports

Volume: 6, P: 1-12
Imaging of influenza virus sialidase activity in living cells

Yuuki Kurebayashi
Tadanobu Takahashi
Takashi Suzuki
ResearchOpen Access02 May 2014
Scientific Reports

Volume: 4, P: 1-7

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