Selected Publications

Structural basis of broad-spectrum β-lactam resistance in Staphylococcus aureus. Alexander JAN, Worrall LJ, Hu J, Vuckovic M, Satishkumar N, Poon R, Sobhanifar S, Rosell FI, Jenkins J, Chiang D, Mosimann WA, Chambers HF, Paetzel M, Chatterjee SS, Strynadka NCJ. (2023) Nature.613(7943):375-382.

Computationally designed peptide macrocycle inhibitors of New Delhi metallo-β-lactamase 1. Mulligan VK, Workman S, Sun T, Rettie S, Li X, Worrall LJ, Craven TW, King DT, Hosseinzadeh P, Watkins AM, Renfrew PD, Guffy S, Labonte JW, Moretti R, Bonneau R, Strynadka NCJ, Baker D. (2021) Proc Natl Acad Sci U S A.118(12):e2012800118.

Structural and kinetic analyses of penicillin-binding protein 4 (PBP4)-mediated antibiotic resistance in Staphylococcus aureus. Alexander JAN, Chatterjee SS, Hamilton SM, Eltis LD, Chambers HF, Strynadka NCJ. (2018) J Biol Chem.293(51):19854-19865.

Crystal structure of New Delhi metallo-β-lactamase reveals molecular basis for antibiotic resistance. King D, Strynadka N. (2011) Protein Sci.20(9):1484-91.

In vitro selection and characterization of ceftobiprole-resistant methicillin-resistant Staphylococcus aureus. Banerjee R, Gretes M, Basuino L, Strynadka N, Chambers HF. (2008) Antimicrob Agents Chemother.52(6):2089-96.

Structural basis for the beta lactam resistance of PBP2a from methicillin-resistant Staphylococcus aureus. Lim D, Strynadka NC. (2002) Nature Struct Biol.9(11):870-6.

Structural Insights into Type III Secretion Systems of the Bacterial Flagellum and Injectisome. Worrall LJ, Majewski DD, Strynadka NCJ. (2023) Annu Rev Microbiol.77:669-698.

Cryo-EM structure of the EspA filament from enteropathogenic Escherichia coli: Revealing the mechanism of effector translocation in the T3SS. Lyons BJE, Atkinson CE, Deng W, Serapio-Palacios A, Finlay BB, Strynadka NCJ. (2021) Structure.29:479-487.e4.

T3S injectisome needle complex structures in four distinct states reveal the basis of membrane coupling and assembly. Hu J, Worrall LJ, Vuckovic M, Hong C, Deng W, Atkinson CE, Finlay BB, Yu Z, Strynadka NCJ. (2019) Nature Microbiol.4(11):2010-2019.

Cryo-EM structure of the homohexameric T3SS ATPase-central stalk complex reveals rotary ATPase-like asymmetry. Majewski DD, Worrall LJ, Hong C, Atkinson CE, Vuckovic M, Watanabe N, Yu Z, Strynadka NCJ. (2019) Nature Commun.10(1):626.

Cryo-EM analysis of the T3S injectisome reveals the structure of the needle and open secretin. Hu J, Worrall LJ, Hong C, Vuckovic M, Atkinson CE, Caveney N, Yu Z, Strynadka NCJ. (2018) Nature Commun.9(1):3840.

Near-atomic-resolution cryo-EM analysis of the Salmonella T3S injectisome basal body. Worrall LJ, Hong C, Vuckovic M, Deng W, Bergeron JRC, Majewski DD, Huang RK, Spreter T, Finlay BB, Yu Z, Strynadka NCJ. (2016) Nature.540(7634):597-601.

Cryo-EM analyses unveil details of mechanism and targocil-II mediated inhibition of S. aureus WTA transporter TarGH. Li FKK, Peters SC, Worrall LJ, Sun T, Hu J, Vuckovic M, Farha M, Palacios A, Caveney NA, Brown ED, Strynadka NCJ. (2025) Nature Commun.16(1):3224.

Cryo-EM characterization of the anhydromuropeptide permease AmpG central to bacterial fitness and β-lactam antibiotic resistance. Sverak HE, Yaeger LN, Worrall LJ, Vacariu CM, Glenwright AJ, Vuckovic M, Al Azawi ZD, Lamers RP, Marko VA, Skorupski C, Soni AS, Tanner ME, Burrows LL, Strynadka NC. (2024) Nature Commun.15(1):9936.

Cryo-EM analysis of S. aureus TarL, a polymerase in wall teichoic acid biogenesis central to virulence and antibiotic resistance. Li FKK, Worrall LJ, Gale RT, Brown ED, Strynadka NCJ. (2024) Sci Adv.9:eadj3864.

CryoEM structure of the antibacterial target PBP1b at 3.3 Å resolution. Caveney NA, Workman SD, Yan R, Atkinson CE, Yu Z, Strynadka NCJ. (2021) Nature Commun.12(1):2775.

Structure and Mechanism of Staphylococcus aureus TarS, the Wall Teichoic Acid β-glycosyltransferase Involved in Methicillin Resistance. Sobhanifar S, Worrall LJ, King DT, Wasney GA, Baumann L, Gale RT, Nosella M, Brown ED, Withers SG, Strynadka NC. (2016) PLoS Pathog.12(12):e1006067.

Structure and mechanism of Staphylococcus aureus TarM, the wall teichoic acid α-glycosyltransferase. Sobhanifar S, Worrall LJ, Gruninger RJ, Wasney GA, Blaukopf M, Baumann L, Lameignere E, Solomonson M, Brown ED, Withers SG, Strynadka NC. (2015) Proc Natl Acad Sci U S A.112(6):E576-85.

An alternative broad-specificity pathway for glycan breakdown in bacteria. Nasseri SA, Lazarski AC, Lemmer IL, Zhang CY, Brencher E, Chen HM, Sim L, Panwar D, Betschart L, Worrall LJ, Brumer H, Strynadka NCJ, Withers SG. (2024) Nature.631(8019):199-206.

X-ray crystallographic characterization of the SARS-CoV-2 main protease polyprotein cleavage sites essential for viral processing and maturation. Lee J, Kenward C, Worrall LJ, Vuckovic M, Gentile F, Ton AT, Ng M, Cherkasov A, Strynadka NCJ, Paetzel M. (2022) Nature Commun.13(1):5196.

Crystallographic structure of wild-type SARS-CoV-2 main protease acyl-enzyme intermediate with physiological C-terminal autoprocessing site. Lee J, Worrall LJ, Vuckovic M, Rosell FI, Gentile F, Ton AT, Caveney NA, Ban F, Cherkasov A, Paetzel M, Strynadka NCJ. (2020) Nature Commun.11(1):5877.

X-ray crystallographic structure of a bacterial polysialyltransferase provides insight into the biosynthesis of capsular polysialic acid. Lizak C, Worrall LJ, Baumann L, Pfleiderer MM, Volkers G, Sun T, Sim L, Wakarchuk W, Withers SG, Strynadka NCJ. (2017) Sci Rep.7(1):5842.

Structure of human ST8SiaIII sialyltransferase provides insight into cell-surface polysialylation. Volkers G, Worrall LJ, Kwan DH, Yu CC, Baumann L, Lameignere E, Wasney GA, Scott NE, Wakarchuk W, Foster LJ, Withers SG, Strynadka NCJ. (2015) Nature Struct Mol Biol.22(8):627-635.

Structural analysis of the alpha-2,3-sialyltransferase Cst-I from Campylobacter jejuni in apo and substrate-analogue bound forms. Chiu CP, Lairson LL, Gilbert M, Wakarchuk WW, Withers SG, Strynadka NC. (2007) Biochemistry.46(24):7196-204.