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Emmanuele Severi

Researcher at University of York

Publications -  21
Citations -  1234

Emmanuele Severi is an academic researcher from University of York. The author has contributed to research in topics: Sialic acid & Periplasmic space. The author has an hindex of 11, co-authored 17 publications receiving 1101 citations. Previous affiliations of Emmanuele Severi include Newcastle University & John Innes Centre.

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Journal ArticleDOI

Sialic acid utilization by bacterial pathogens

TL;DR: This mini-review will summarize recent findings relating to sialic acid transport, modification of sialing acid by O-acetylation, and the mechanisms of sIALic acid-mediated complement resistance.
Journal ArticleDOI

Ammonium sensing in Escherichia coli: role of the ammonium transporter AmtB and AmtB-GlnK complex formation

TL;DR: It is shown that Escherichia coli AmtB is inactivated by formation of a membrane-bound complex with GlnK, which provides an exquisitely sensitive mechanism to control ammonium flux into the cell, and the conservation of glnK linkage to amtB suggests that this regulatory mechanism may occur throughout prokaryotes.
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Sialic acid transport in Haemophilus influenzae is essential for lipopolysaccharide sialylation and serum resistance and is dependent on a novel tripartite ATP‐independent periplasmic transporter

TL;DR: It is demonstrated that N‐acetylneuraminic acid (Neu5Ac or sialic acid) uptake in H.’influenzae is essential for the subsequent modification of the LPS and that this uptake is mediated through a single transport system which is a member of the tripartite ATP‐independent periplasmic (TRAP) transporter family.
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The substrate-binding protein imposes directionality on an electrochemical sodium gradient-driven TRAP transporter.

TL;DR: The membrane reconstitution of a TRAP transporter, the sialic acid-specific SiaPQM system from Haemophilus influenzae, is reported, and its mechanism of energy coupling is elucidated.
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Conservation of Structure and Mechanism in Primary and Secondary Transporters Exemplified by Siap, a Sialic Acid Binding Virulence Factor from Haemophilus Influenzae

TL;DR: The structure of SiaP reveals an overall topology similar to ATP binding cassette ESR proteins, which is not apparent from the sequence, demonstrating that primary and secondary transporters can share a common structural component.