Effect of β-propiolactone — an inhibitor of HTLV III/LAV activity — on immunological analyses

Ball, M.J.; Spriggs, V.; Sutton, Paul M.; Chapel, Helen

doi:10.1016/0022-1759(86)90324-8

Cited by 10 publications

(6 citation statements)

References 4 publications

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“…This is consistent with Ball et al, 9 who showed a non-significant fall from 2870 to 2770 mg/litre after approximately three hours at a β propiolactone concentration of 0.25%. LoGrippo 4 measured the α1 region on electrophoresis in three samples containing 0.35% β propiolactone, and found a decrease of greater than 10% compared with the untreated samples, but not for samples treated with both β propiolactone and ultraviolet irradiation.…”

Section: Discussionsupporting

confidence: 92%

“…8 Ball et al showed that a concentration of β propiolactone of 0.25% had no effect on a wide range of laboratory tests. 9 Recently, we have started to add β propiolactone at a concentration of 0.5% (Sigma, Poole, Dorset, UK; product code P5648; formula C 3 H 4 O 2 ) to high risk sera for protein electrophoresis and nephelometry. A laboratory error was suspected when three consecutive high risk sera showed a complete absence of the α1 band on electrophoresis using Sebia's automated Hydrasys system (fig 1).…”

mentioning

confidence: 99%

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Effect of beta propiolactone viral inactivation on alpha1 antitrypsin values

Katona

Bowen²,

Kaminski³

2002

Journal of Clinical Pathology

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Aims: α1 Antitrypsin was undetectable in several patient samples treated with 0.5% β propiolactone, which was used as a virucidal agent. This study was designed to confirm β propiolactone as the cause and determine why it might have such an effect. Methods: Volumes of 0, 5, 10, and 20 µl of β propiolactone were added to 2 ml aliquots of serum to make final concentrations of 0%, 0.25%, 0.5%, and 1% of β propiolactone. α1 Antitrypsin concentrations and the pH were measured at different time intervals. The effects of adding buffer before the addition of β propiolactone, NaOH after β propiolactone, and 6M HCl instead of β propiolactone were also measured.Results: The addition of β propiolactone to a volunteer's serum showed a fall in both α1 antitrypsin values and pH with increasing time and concentration of β propiolactone. This effect was also seen when adding HCl, but was partially prevented by buffering the serum or adding NaOH. Conclusions: These results suggest that it is the acidity of the degradation products of β propiolactone that is responsible for the fall in α1 antitrypsin values. This fall in α1 antitrypsin values was dependent on the concentration of β propiolactone used and the length of time before the test was performed. The effect of β propiolactone on laboratory tests should be re-evaluated, with attention being paid to sample pH, storage time, and storage temperature.

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Section: Discussionsupporting

confidence: 92%

mentioning

confidence: 99%

Effect of beta propiolactone viral inactivation on alpha1 antitrypsin values

Katona

Bowen²,

Kaminski³

2002

Journal of Clinical Pathology

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“…So far, studies investigating the effect of BPL on downstream assays have come to diverging conclusions. Ball et al tested the effects of BPL on immunological analysis of various blood components of common interest in the context of HIV infection . They tested for G, A, and M class immunoglobulins, complement components C3 and C4, haptoglobin, α1-antitrypsin, C-reactive protein, and others using a Beckman Immunochemistry Analysis System.…”

Section: Introductionmentioning

confidence: 99%

“…Ball et al tested the effects of BPL on immunological analysis of various blood components of common interest in the context of HIV infection. 3 They tested for G, A, and M class immunoglobulins, complement components C3 and C4, haptoglobin, α1antitrypsin, C-reactive protein, and others using a Beckman Immunochemistry Analysis System. Measured plasma concentrations of these proteins did not change significantly following BPL treatment.…”

Section: ■ Introductionmentioning

confidence: 99%

Sample-Treatment with the Virucidal β-Propiolactone Does Not Preclude Analysis by Large Panel Affinity Proteomics, Including the Discovery of Biomarker Candidates

Beutgen,

Bhagwat,

Steitz

et al. 2024

Anal. Chem.

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Virus inactivation is a prerequisite for safe handling of high-risk infectious samples. β-Propiolactone (BPL) is an established reagent with proven virucidal efficacy. BPL primarily reacts with DNA, RNA, and amino acids. The latter may modify antigenic protein epitopes interfering with binding properties of affinity reagents such as antibodies and aptamers used in affinity proteomic screens. We investigated (i) the impact of BPL treatment on the analysis of protein levels in plasma samples using the aptamer-based affinity proteomic platform SomaScan and (ii) effects on protein detection in conditioned medium samples using the proximity extension assay-based Olink Target platform. In the former setup, BPL-treated and native plasma samples from patients with ovarian cancer (n = 12) and benign diseases (n = 12) were analyzed using the SomaScan platform. In the latter, conditioned media samples collected from cultured T cells with (n = 3) or without (n = 3) anti-CD3 antibody stimulation were analyzed using the Olink Target platform. BPL-related changes in protein detection were evaluated comparing native and BPL-treated states, simulating virus inactivation, and impact on measurable group differences was assessed. While approximately one-third of SomaScan measurements were significantly changed by the BPL treatment, a majority of antigen/aptamer interactions remained unaffected. Interaction effects of BPL treatment and disease state, potentially altering detectability of group differences, were observable for less than one percent of targets (0.6%). BPL effects on protein detection with Olink Target were also limited, affecting 3.6% of detected proteins with no observable interaction effects. Thus, effects of BPL treatment only moderately interfere with affinity proteomic detectability of differential protein expression between different experimental groups. Overall, the results prove high-throughput affinity proteomics well suited for the analysis of high-risk samples inactivated using BPL.

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“…6 us..'iingAPAP echnqu.Thsatbd use and clearpositivity shows that BPL has had e.ffect on antigen expression.…”

mentioning

confidence: 99%

Use of betapropiolactone to disinfect fresh tissue without impairing antigenicity: method applicable to human immunodeficiency virus (HIV) positive tissue.

Chaplin

Heryet²,

Holdsworth³

et al. 1989

Journal of Clinical Pathology

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Effect of β-propiolactone — an inhibitor of HTLV III/LAV activity — on immunological analyses

Cited by 10 publications

References 4 publications

Effect of beta propiolactone viral inactivation on alpha1 antitrypsin values

Effect of beta propiolactone viral inactivation on alpha1 antitrypsin values

Sample-Treatment with the Virucidal β-Propiolactone Does Not Preclude Analysis by Large Panel Affinity Proteomics, Including the Discovery of Biomarker Candidates

Use of betapropiolactone to disinfect fresh tissue without impairing antigenicity: method applicable to human immunodeficiency virus (HIV) positive tissue.

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