Definition and research guide
This page combines a MeSH definition, publication statistics and selected research abstracts. It is a starting point for reading the literature, not a medical textbook or a systematic evidence review.
Content available: 4 complete abstracts (756 words), 10 references. Full article text is not stored or reproduced here; follow the PMID, DOI or PMC links to read the original sources and their access terms.
Definition
The measurement of infection-blocking titer of antisera by testing a series of dilutions for a given virus-antiserum interaction end-point, which is generally the dilution at which tissue cultures inoculated with the serum-virus mixtures demonstrate cytopathology (CPE) or the dilution at which 50% of test animals injected with serum-virus mixtures show infectivity (ID50) or die (LD50).
Definition: NLM Medical Subject Headings (MeSH) scope note (Public domain (U.S. National Library of Medicine); attribution requested). View the MeSH record.
Also known as: Neutralization Test; Test, Neutralization; Tests, Neutralization.
Where it fits in the MeSH classification
- Broader topics
- Serologic Tests
- See also
- Antibodies, Neutralizing
Related concepts
Research landscape
PubMed indexes 26,165 records tagged with the MeSH heading “Neutralization Tests” (counts retrieved 2026-11-04). 1,850 of them (7.1%) were published from 2020 onward, and the busiest period so far is through 1999 with 15,934 records.
Reviews account for 553 records (2.1%) and meta-analyses for 8. Randomized controlled trials number 348 (1.3%) as a share of all records on the topic. Randomized trials make up only a small share of this literature, so much of what is known comes from laboratory, observational or descriptive work.
Show the data
| Period | Records |
|---|---|
| through 1999 | 15,934 |
| 2000-2009 | 4,821 |
| 2010-2019 | 3,560 |
| 2020 onward | 1,850 |
Publication-type chart data
| Type | Records | Share |
|---|---|---|
| Reviews | 553 | 2.1% |
| Meta-analyses | 8 | 0.0% |
| Randomized controlled trials | 348 | 1.3% |
Method: PubMed query "Neutralization Tests"[MeSH Terms] with publication-type and date filters, retrieved 2026-11-04.
Reading the evidence in diagnostics and medical technology
A test or device is judged by how well it detects a condition, how often it gives false alarms or misses cases, and whether using it improves outcomes for people. Accuracy depends on who is tested and how common the condition is, so a test that performs well in a specialist hospital can perform differently in the community. Check the reference standard, the population studied, the sensitivity and specificity and whether results were confirmed in a separate group.
Evidence from open-access studies
These open-access studies come from PubMed’s best-match results for this heading (papers whose main topic it is), ranked here by citation count, with one recent addition. Each abstract is reproduced in full under its recorded open licence so that you can read the authors’ own words. They illustrate the literature; they are not a systematic summary of it. Citation counts measure attention, not reliability or clinical benefit.
| Study / authors | Year | Source label / design | Europe PMC citations | Licence / source |
|---|---|---|---|---|
| Omicron escapes the majority of existing SARS-CoV-2 neutralizing antibodies | 2022 | Research article Design not recorded in structured metadata | 1,799 | cc by PMID 35016194 · DOI · PMC8866119 |
| Omicron extensively but incompletely escapes Pfizer BNT162b2 neutralization | 2022 | Research article Design not recorded in structured metadata | 1,050 | cc by PMID 35016196 · DOI · PMC8866126 |
| Protocol and Reagents for Pseudotyping Lentiviral Particles with SARS-CoV-2 Spike Protein for Neutralization Assays | 2020 | Research article Design not recorded in structured metadata | 825 | cc by PMID 32384820 · DOI · PMC7291041 |
| Organoid-based neutralization assays reveal a distinctive profile of SARS-CoV-2 antibodies and recapitulate the real-world efficacy | 2025 | Research article Design not recorded in structured metadata | 8 | cc by PMID 40875807 · DOI · PMC12415223 |
Omicron escapes the majority of existing SARS-CoV-2 neutralizing antibodies [1]
Abstract reading summary — source excerpts
- Opening excerpt
- The SARS-CoV-2 B.
- Closing excerpt
- Our results inform the development of antibody-based drugs and vaccines against Omicron and future variants.
- Interpretation limits
- Verbatim excerpts from the authors’ abstract; the closing excerpt may describe a finding, limitation or recommendation. Design, population, effect size and uncertainty have not been independently extracted or appraised. Read the complete abstract and linked paper before interpreting the findings.
Read complete abstract (257 words)
The SARS-CoV-2 B.1.1.529 (Omicron) variant contains 15 mutations of the receptor-binding domain (RBD). How Omicron evades RBD-targeted neutralizing antibodies requires immediate investigation. Here we use high-throughput yeast display screening1,2 to determine the profiles of RBD escaping mutations for 247 human anti-RBD neutralizing antibodies and show that the neutralizing antibodies can be classified by unsupervised clustering into six epitope groups (A-F)-a grouping that is highly concordant with knowledge-based structural classifications3-5. Various single mutations of Omicron can impair neutralizing antibodies of different epitope groups. Specifically, neutralizing antibodies in groups A-D, the epitopes of which overlap with the ACE2-binding motif, are largely escaped by K417N, G446S, E484A and Q493R. Antibodies in group E (for example, S309)6 and group F (for example, CR3022)7, which often exhibit broad sarbecovirus neutralizing activity, are less affected by Omicron, but a subset of neutralizing antibodies are still escaped by G339D, N440K and S371L. Furthermore, Omicron pseudovirus neutralization showed that neutralizing antibodies that sustained single mutations could also be escaped, owing to multiple synergetic mutations on their epitopes. In total, over 85% of the tested neutralizing antibodies were escaped by Omicron. With regard to neutralizing-antibody-based drugs, the neutralization potency of LY-CoV016, LY-CoV555, REGN10933, REGN10987, AZD1061, AZD8895 and BRII-196 was greatly undermined by Omicron, whereas VIR-7831 and DXP-604 still functioned at a reduced efficacy. Together, our data suggest that infection with Omicron would result in considerable humoral immune evasion, and that neutralizing antibodies targeting the sarbecovirus conserved region will remain most effective. Our results inform the development of antibody-based drugs and vaccines against Omicron and future variants.
Abstract reproduced from the open-access article under the recorded cc by licence; © the authors. PMID 35016194 · DOI · PMC8866119
Omicron extensively but incompletely escapes Pfizer BNT162b2 neutralization [2]
Abstract reading summary — source excerpts
- Opening excerpt
- The emergence of the SARS-CoV-2 variant of concern Omicron (Pango lineage B.
- Closing excerpt
- These data support the notion that reasonable protection against Omicron may be maintained using vaccination approaches.
- Interpretation limits
- Verbatim excerpts from the authors’ abstract; the closing excerpt may describe a finding, limitation or recommendation. Design, population, effect size and uncertainty have not been independently extracted or appraised. Read the complete abstract and linked paper before interpreting the findings.
Read complete abstract (186 words)
The emergence of the SARS-CoV-2 variant of concern Omicron (Pango lineage B.1.1.529), first identified in Botswana and South Africa, may compromise vaccine effectiveness and lead to re-infections1. Here we investigated Omicron escape from neutralization by antibodies from South African individuals vaccinated with Pfizer BNT162b2. We used blood samples taken soon after vaccination from individuals who were vaccinated and previously infected with SARS-CoV-2 or vaccinated with no evidence of previous infection. We isolated and sequence-confirmed live Omicron virus from an infected person and observed that Omicron requires the angiotensin-converting enzyme 2 (ACE2) receptor to infect cells. We compared plasma neutralization of Omicron relative to an ancestral SARS-CoV-2 strain and found that neutralization of ancestral virus was much higher in infected and vaccinated individuals compared with the vaccinated-only participants. However, both groups showed a 22-fold reduction in vaccine-elicited neutralization by the Omicron variant. Participants who were vaccinated and had previously been infected exhibited residual neutralization of Omicron similar to the level of neutralization of the ancestral virus observed in the vaccination-only group. These data support the notion that reasonable protection against Omicron may be maintained using vaccination approaches.
Abstract reproduced from the open-access article under the recorded cc by licence; © the authors. PMID 35016196 · DOI · PMC8866126
Protocol and Reagents for Pseudotyping Lentiviral Particles with SARS-CoV-2 Spike Protein for Neutralization Assays [3]
Abstract reading summary — source excerpts
- Opening excerpt
- SARS-CoV-2 enters cells using its Spike protein, which is also the main target of neutralizing antibodies.
- Closing excerpt
- Furthermore, we demonstrated how these pseudotyped lentiviral particles could be used to measure the neutralizing activity of human sera or plasma against SARS-CoV-2 in convenient luciferase-based assays, thereby providing a valuable complement to ELISA-based methods that measure antibody binding rather than neutralization.
- Interpretation limits
- Verbatim excerpts from the authors’ abstract; the closing excerpt may describe a finding, limitation or recommendation. Design, population, effect size and uncertainty have not been independently extracted or appraised. Read the complete abstract and linked paper before interpreting the findings.
Read complete abstract (162 words)
SARS-CoV-2 enters cells using its Spike protein, which is also the main target of neutralizing antibodies. Therefore, assays to measure how antibodies and sera affect Spike-mediated viral infection are important for studying immunity. Because SARS-CoV-2 is a biosafety-level-3 virus, one way to simplify such assays is to pseudotype biosafety-level-2 viral particles with Spike. Such pseudotyping has now been described for single-cycle lentiviral, retroviral, and vesicular stomatitis virus (VSV) particles, but the reagents and protocols are not widely available. Here, we detailed how to effectively pseudotype lentiviral particles with SARS-CoV-2 Spike and infect 293T cells engineered to express the SARS-CoV-2 receptor, ACE2. We also made all the key experimental reagents available in the BEI Resources repository of ATCC and the NIH. Furthermore, we demonstrated how these pseudotyped lentiviral particles could be used to measure the neutralizing activity of human sera or plasma against SARS-CoV-2 in convenient luciferase-based assays, thereby providing a valuable complement to ELISA-based methods that measure antibody binding rather than neutralization.
Abstract reproduced from the open-access article under the recorded cc by licence; © the authors. PMID 32384820 · DOI · PMC7291041
Organoid-based neutralization assays reveal a distinctive profile of SARS-CoV-2 antibodies and recapitulate the real-world efficacy [4]
Abstract reading summary — source excerpts
- Opening excerpt
- The efficacy of VIR-7831, a class 3 anti-SARS-CoV-2 monoclonal antibody (mAb), was demonstrated repeatedly in clinical trials; yet, reduced neutralization against Omicron variants in cell-line-based neutralization assays led to its withdrawal from clinical use.
- Closing excerpt
- The organoid-based neutralization assays, superior to conventional cell-line-based assays, can recapitulate and predict the real-world efficacy of mAbs.
- Interpretation limits
- Verbatim excerpts from the authors’ abstract; the closing excerpt may describe a finding, limitation or recommendation. Design, population, effect size and uncertainty have not been independently extracted or appraised. Read the complete abstract and linked paper before interpreting the findings.
Read complete abstract (151 words)
The efficacy of VIR-7831, a class 3 anti-SARS-CoV-2 monoclonal antibody (mAb), was demonstrated repeatedly in clinical trials; yet, reduced neutralization against Omicron variants in cell-line-based neutralization assays led to its withdrawal from clinical use. We developed organoid-based neutralization assays to measure mAb potency. We found that most class 3 mAbs, especially those not blocking receptor-binding domain-ACE2 binding, including VIR-7831, were substantially underestimated in cell-line-based assays. Nasal organoids adequately recapitulated the real-world effectiveness of VIR-7831 because of biologically relevant low ACE2 expression, and exclusively reproduced the in vivo protection of S2 mAbs due to the high TMPRSS2 expression, reminiscent of native human respiratory epithelial cells. Collectively, the robust organoid culture system and biologically relevant expression profiles of ACE2 and TMPRSS2 make nasal organoids present a correlate of in vivo protection of neutralizing mAbs exclusively. The organoid-based neutralization assays, superior to conventional cell-line-based assays, can recapitulate and predict the real-world efficacy of mAbs.
Abstract reproduced from the open-access article under the recorded cc by licence; © the authors. PMID 40875807 · DOI · PMC12415223
Key reviews and meta-analyses
The most cited review-type papers among PubMed’s best-match results for this heading, listed with bibliographic details only. Follow the links for the full text and access terms.
- Research article Broadly neutralizing antiviral antibodies [5]
- Research article Guidelines for Plaque-Reduction Neutralization Testing of Human Antibodies to Dengue Viruses [6]
- Research article Recent advances in the characterization of HIV-1 neutralization assays for standardized evaluation of the antibody response to infection and vaccination [7]
- Research article A multi-hit model for the neutralization of animal viruses [8]
- Research article Antigenic variation in foot-and-mouth disease: studies based on the virus neutralization reaction [9]
- Research article Antibody neutralization of HIV-1 [10]
References
- Cao Y, Wang J, Jian F, Xiao T, Song W, Yisimayi A, et al.. Omicron escapes the majority of existing SARS-CoV-2 neutralizing antibodies. . 2022. PMID 35016194 · DOI · PMC8866119
- Cele S, Jackson L, Khoury DS, Khan K, Moyo-Gwete T, Tegally H, et al.. Omicron extensively but incompletely escapes Pfizer BNT162b2 neutralization. . 2022. PMID 35016196 · DOI · PMC8866126
- Crawford KHD, Eguia R, Dingens AS, Loes AN, Malone KD, Wolf CR, et al.. Protocol and Reagents for Pseudotyping Lentiviral Particles with SARS-CoV-2 Spike Protein for Neutralization Assays. . 2020. PMID 32384820 · DOI · PMC7291041
- Wan Z, Li C, Zhou Y, Yu Y, Chiu MC, Huang J, et al.. Organoid-based neutralization assays reveal a distinctive profile of SARS-CoV-2 antibodies and recapitulate the real-world efficacy. . 2025. PMID 40875807 · DOI · PMC12415223
- Corti D, Lanzavecchia A. Broadly neutralizing antiviral antibodies. Annu Rev Immunol. 2013. PMID 23330954 · DOI
- Roehrig JT, Hombach J, Barrett AD. Guidelines for Plaque-Reduction Neutralization Testing of Human Antibodies to Dengue Viruses. Viral Immunol. 2008. PMID 18476771 · DOI
- Polonis VR, Brown BK, Rosa Borges A, Zolla-Pazner S, Dimitrov DS, Zhang MY, et al.. Recent advances in the characterization of HIV-1 neutralization assays for standardized evaluation of the antibody response to infection and vaccination. Virology. 2008. PMID 18367229 · DOI
- Della-Porta AJ, Westaway EG. A multi-hit model for the neutralization of animal viruses. J Gen Virol. 1978. PMID 74400 · DOI
- Rweyemamu MM. Antigenic variation in foot-and-mouth disease: studies based on the virus neutralization reaction. J Biol Stand. 1984. PMID 6207176 · DOI
- Poignard P, Klasse PJ, Sattentau QJ. Antibody neutralization of HIV-1. Immunol Today. 1996. PMID 8991386 · DOI
About this article
- Sources
- NLM Medical Subject Headings (definition, synonyms); NCBI PubMed (counts, identifiers); Europe PMC (open-access abstracts and citation counts).
- Verification
- Every reference was resolved against PubMed on 2026-11-04; title, year and DOI matched.
- Review state
- automated source verified; no human expert review has been recorded yet.
- Version
- 1, last updated 2026-11-04.
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Evidence strength
EvidenceHelix's computed view of the study designs behind this topic: how common meta-analyses, randomized trials and reviews are, how recent the literature is, and a plain-language reading. It describes the design mix of the literature. It is not a quality appraisal of any study, and it is not medical advice.