Evidence map›Paper›PMID 36284469›Full record

ArticlemAbs

Insights into ultra-low affinity lipase-antibody noncovalent complex binding mechanisms.

Elizabeth Sara Hecht, Shrenik Mehta, Aaron T Wecksler, Ben Aguilar, Nathaniel Swanson, Wilson Phung, Ananya Dubey Kelsoe, W Henry Benner, Devin Tesar, Robert F Kelley and 2 more

Open access · goldAbstract read
In one paragraph

Article in mAbs. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
2.8field-weighted citation impact, top 9% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

11 citing papers in PubMed, 18 citations in OpenAlex.

  1. Review
  2. Review
  3. Analytical Tools for HCP Detection, Identification, and Quantitation.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  4. Article
  5. Recent insight into the advances and prospects of microbial lipases and their potential applications in industry.International microbiology : the official journal of the Spanish Society for Microbiology · 2024
    Review
  6. Review
  7. Review
  8. Dissecting the structural heterogeneity of proteins by native mass spectrometry.Protein science : a publication of the Protein Society · 2023
    Review
  9. Review
  10. Review
  11. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

12 authors.

Elizabeth Sara HechtMicrochemistry, Proteomics, and Lipidomics, Genentech, Inc South San Francisco, CA, USA.
Shrenik MehtaPharmaceutical Development, Genentech, Inc South San Francisco, CA, USA.
Aaron T WeckslerProtein Analytical Chemistry, Genentech, Inc South San Francisco, CA, USA.
Ben AguilarIonDX, Inc Monterey, CA, USA.
Nathaniel SwansonPharmaceutical Development, Genentech, Inc South San Francisco, CA, USA.
Wilson PhungMicrochemistry, Proteomics, and Lipidomics, Genentech, Inc South San Francisco, CA, USA.
Ananya Dubey KelsoeIonDX, Inc Monterey, CA, USA.
W Henry BennerIonDX, Inc Monterey, CA, USA.
Devin TesarPharmaceutical Development, Genentech, Inc South San Francisco, CA, USA.
Robert F KelleyPharmaceutical Development, Genentech, Inc South San Francisco, CA, USA.
Wendy SandovalMicrochemistry, Proteomics, and Lipidomics, Genentech, Inc South San Francisco, CA, USA.ORCID 0000-0002-4672-0762
Alavattam SreedharaPharmaceutical Development, Genentech, Inc South San Francisco, CA, USA.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Detection of host cell protein (HCP) impurities is critical to ensuring that recombinant drug products, including monoclonal antibodies (mAbs), are safe. Mechanistic characterization as to how HCPs persist in drug products is important to refining downstream processing. It has been hypothesized that weak lipase-mAb interactions enable HCP lipases to evade drug purification processes. Here, we apply state-of-the-art methods to establish lipase-mAb binding mechanisms. First, the mass spectrometry (MS) approach of fast photochemical oxidation of proteins was used to elucidate putative binding regions. The CH1 domain was identified as a conserved interaction site for IgG1 and IgG4 mAbs against the HCPs phospholipase B-like protein (PLBL2) and lysosomal phospholipase A2 (LPLA2). Rationally designed mutations in the CH1 domain of the IgG4 mAb caused a 3- to 70-fold K

Indexed as

LysophospholipaseSphingomyelin PhosphodiesteraseAcetonitrilesAnimalsAntibodies, MonoclonalCHO CellsCricetinaeCricetulusDithiothreitolGlycoside HydrolasesHumansImmunoglobulin GLipaseMannoseMethanolPhospholipases A2AcetonitrilesAntibodies, MonoclonalDithiothreitolGlycoside HydrolasesImmunoglobulin GLipaseLysophospholipaseMannoseMethanolPhospholipases A2PolysorbatesSphingomyelin PhosphodiesteraseTrifluoroacetic AcidantibodybindingFPOPlipasenative mass spectrometrypolysorbateprotein complex

Identifiers

PMID36284469
PMCPMC9621051
OpenAlexW4307426874

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.