The University of Southampton
University of Southampton Institutional Repository

A cold water, ultrasonically activated stream efficiently removes proteins and prion-associated amyloid from surgical stainless steel: ultrasonic water stream for surgical decontamination

A cold water, ultrasonically activated stream efficiently removes proteins and prion-associated amyloid from surgical stainless steel: ultrasonic water stream for surgical decontamination
A cold water, ultrasonically activated stream efficiently removes proteins and prion-associated amyloid from surgical stainless steel: ultrasonic water stream for surgical decontamination

Background: Sterile service department decontamination procedures for surgical instruments struggle to demonstrate efficient removal of the hardiest infectious contaminants, such as prion proteins. A recently designed novel system, which uses a low pressure ultrasonically activated, cold water stream, has previously demonstrated efficient hard surface cleaning of several biological contaminants. Aim: To test the efficacy of an ultrasonically activated stream for the removal of tissue proteins, including prion-associated amyloid, from surgical stainless steel surfaces. Methods: Test surfaces were contaminated with 22L, ME7 or 263K prion-infected brain homogenates. The surfaces were treated with the ultrasonically activated water stream for contact times of 5 and 10 s. Residual proteinaceous and amyloid contamination were quantified using sensitive microscopic analysis, and immunoblotting was used to characterize the eluted prion residues before and after treatment with the ultrasonically activated stream. Findings: Efficient removal of the different prion strains from the surgical stainless steel surfaces was observed, and reduced levels of protease-susceptible and -resistant prion protein was detected in recovered supernatant. Conclusion: This study demonstrated that an ultrasonically activated stream has the potential to be a cost-effective solution to improve current decontamination practices and has the potential to reduce hospital-acquired infections.

Creutzfeldt–Jakob disease, Decontamination, Prion, Protein, Surgical, Ultrasonic cleaning
0195-6701
649-656
Secker, T.J.
16b0a878-984f-4272-bfaa-667c7c63023a
Leighton, Timothy
3e5262ce-1d7d-42eb-b013-fcc5c286bbae
Offin, Douglas
69c8edbf-8848-4346-941a-65b381a365c2
Birkin, Peter R.
ba466560-f27c-418d-89fc-67ea4f81d0a7
Herve, Rodolphe
9baddc65-93cf-4a18-9388-088d60572b06
Keevil, Charles
cb7de0a7-ce33-4cfa-af52-07f99e5650eb
Secker, T.J.
16b0a878-984f-4272-bfaa-667c7c63023a
Leighton, Timothy
3e5262ce-1d7d-42eb-b013-fcc5c286bbae
Offin, Douglas
69c8edbf-8848-4346-941a-65b381a365c2
Birkin, Peter R.
ba466560-f27c-418d-89fc-67ea4f81d0a7
Herve, Rodolphe
9baddc65-93cf-4a18-9388-088d60572b06
Keevil, Charles
cb7de0a7-ce33-4cfa-af52-07f99e5650eb

Secker, T.J., Leighton, Timothy, Offin, Douglas, Birkin, Peter R., Herve, Rodolphe and Keevil, Charles (2020) A cold water, ultrasonically activated stream efficiently removes proteins and prion-associated amyloid from surgical stainless steel: ultrasonic water stream for surgical decontamination. Journal of Hospital Infection, 106 (4), 649-656. (doi:10.1016/j.jhin.2020.09.021).

Record type: Article

Abstract

Background: Sterile service department decontamination procedures for surgical instruments struggle to demonstrate efficient removal of the hardiest infectious contaminants, such as prion proteins. A recently designed novel system, which uses a low pressure ultrasonically activated, cold water stream, has previously demonstrated efficient hard surface cleaning of several biological contaminants. Aim: To test the efficacy of an ultrasonically activated stream for the removal of tissue proteins, including prion-associated amyloid, from surgical stainless steel surfaces. Methods: Test surfaces were contaminated with 22L, ME7 or 263K prion-infected brain homogenates. The surfaces were treated with the ultrasonically activated water stream for contact times of 5 and 10 s. Residual proteinaceous and amyloid contamination were quantified using sensitive microscopic analysis, and immunoblotting was used to characterize the eluted prion residues before and after treatment with the ultrasonically activated stream. Findings: Efficient removal of the different prion strains from the surgical stainless steel surfaces was observed, and reduced levels of protease-susceptible and -resistant prion protein was detected in recovered supernatant. Conclusion: This study demonstrated that an ultrasonically activated stream has the potential to be a cost-effective solution to improve current decontamination practices and has the potential to reduce hospital-acquired infections.

Text
A cold water, ultrasonic activated stream - Accepted Manuscript
Download (4MB)

More information

Accepted/In Press date: 11 September 2020
e-pub ahead of print date: 19 September 2020
Published date: December 2020
Additional Information: Copyright © 2020 The Healthcare Infection Society. Published by Elsevier Ltd. All rights reserved.
Keywords: Creutzfeldt–Jakob disease, Decontamination, Prion, Protein, Surgical, Ultrasonic cleaning

Identifiers

Local EPrints ID: 444080
URI: http://eprints.soton.ac.uk/id/eprint/444080
ISSN: 0195-6701
PURE UUID: 6b1e6b35-8de6-4663-be69-0448c118cdf8
ORCID for T.J. Secker: ORCID iD orcid.org/0000-0001-7168-8592
ORCID for Timothy Leighton: ORCID iD orcid.org/0000-0002-1649-8750
ORCID for Peter R. Birkin: ORCID iD orcid.org/0000-0002-6656-4074
ORCID for Rodolphe Herve: ORCID iD orcid.org/0000-0001-8838-6515
ORCID for Charles Keevil: ORCID iD orcid.org/0000-0003-1917-7706

Catalogue record

Date deposited: 24 Sep 2020 16:40
Last modified: 17 Mar 2024 05:55

Export record

Altmetrics

Contributors

Author: T.J. Secker ORCID iD
Author: Douglas Offin
Author: Peter R. Birkin ORCID iD
Author: Rodolphe Herve ORCID iD
Author: Charles Keevil ORCID iD

Download statistics

Downloads from ePrints over the past year. Other digital versions may also be available to download e.g. from the publisher's website.

View more statistics

Atom RSS 1.0 RSS 2.0

Contact ePrints Soton: eprints@soton.ac.uk

ePrints Soton supports OAI 2.0 with a base URL of http://eprints.soton.ac.uk/cgi/oai2

This repository has been built using EPrints software, developed at the University of Southampton, but available to everyone to use.

We use cookies to ensure that we give you the best experience on our website. If you continue without changing your settings, we will assume that you are happy to receive cookies on the University of Southampton website.

×