All reviews of published articles are made public. This includes manuscript files, peer review comments, author rebuttals and revised materials. Note: This was optional for articles submitted before 13 February 2023.
Peer reviewers are encouraged (but not required) to provide their names to the authors when submitting their peer review. If they agree to provide their name, then their personal profile page will reflect a public acknowledgment that they performed a review (even if the article is rejected). If the article is accepted, then reviewers who provided their name will be associated with the article itself.
The paper is accepted on the reviewer recommendations
[# PeerJ Staff Note - this decision was reviewed and approved by Vladimir Uversky, a PeerJ Section Editor covering this Section #]
The investigation of glycan profiles and glycosyltransferase expression in benign and malignant meningiomas contributes significantly to our understanding of the molecular changes underlying these tumors, potentially paving the way for novel diagnostic and therapeutic strategies.
Experiments are meticulously planned.
The study looks into the functional implications of altered glycosylation in malignant meningiomas, raising important questions about tumor behavior and immune responses. Furthermore, the clinical significance of the study, which investigates how identified glycosylation changes can be used for diagnostics and therapeutics, emphasizes its potential translational impact and aligns with current trends in personalized medicine.
No comment
No comment
No comment
As I see the following needs to be done prior to taking up for a
1. The introduction needs the latest references
2. thoroughly revision for grammatical errors is a concern to all reviewers
3. rationale behind the study and statistical significance
**PeerJ Staff Note:** Please ensure that all review, editorial, and staff comments are addressed in a response letter and any edits or clarifications mentioned in the letter are also inserted into the revised manuscript where appropriate.
**Language Note:** The Academic Editor has identified that the English language must be improved. PeerJ can provide language editing services - please contact us at copyediting@peerj.com for pricing (be sure to provide your manuscript number and title). Alternatively, you should make your own arrangements to improve the language quality and provide details in your response letter. – PeerJ Staff
The manuscript provides a comprehensive overview of research concerning alterations in protein glycosylation in meningiomas.
The experiments in the study were meticulously conducted; however, it appears that the research did not introduce novel findings to the existing literature.
1. The identification of highly expressed terminal galactose (Gal) and N-acetyl galactosamine (GalNAc) in primary benign meningioma cells in contrast to malignant meningioma cell lines could potentially constitute a novel observation. However, conclusive evidence necessitates further validation.
2. The mention of aberrant mucin types of O-glycosylations in meningiomas, as observed through the GEO database and mRNA experiments (COSMC, MUC1, C2GNT2, ST3GAL1, ST3GAL3, FUT1, and FUT8) in malignant meningiomas compared to benign cell lines are important.
It is essential to acknowledge the extensive literature available on these topics.
While it is evident that the authors have conducted a thorough analysis and have unveiled several significant findings, it is imperative to ascertain whether these findings represent entirely novel contributions or if they have been previously documented in the literature.
A few concerns require the author's attention:
Definition of Meningioma Grades: The manuscript does not clearly define meningioma cell lines into Grade I, Grade II, and Grade III.
Absence of a Grade II Cell Line: A discrepancy arises from the assertion made on lines 24 and 25 of the manuscript regarding the utilization of Grade II cell lines, as there seems to be an absence of detailed reference to this particular grade in subsequent descriptions.
Please switch the columns and rows in Figure 1 to improve the data presentation
Grammatical errors and factually inaccurate statements are major flaws in this manuscript.
There are a lot of grammatical errors, often resulting in scientifically inaccurate sentences. For example, while talking about the changes in protein levels, authors incorrectly talk about changes in glycosylation – protein levels and glycosylation are completely different and not interchangeable concepts.
The sample size is very small.
The authors do not explain the scientific rationale for any of their experimental decisions well. For example, why do authors feel Lectin cytochemistry is the best way to analyze the changes in O-glycosylation?
The study is highly biased and, therefore, doesn’t add much value to the field.
Proper statistical analyses are missing.
The title is misleading – the authors do not measure O-linked glycosylation. Mass spectrometry would be a better approach for such analysis. If authors wish to try to resubmit, it will require significantly more work – particularly the mass spec analysis to provide a comprehensive overview of changes in O-linked glycosylation
Please perform a literature search and make sure to include relevant papers. Elaborate how the current study is different compared to other similar papers.
Language used for the manuscript is clear and professional. Introduction and background are provided to describe the research topic. All figures are supplied with clear labels and descriptions. The basic reporting of the manuscript is decent.
First comment is that the research question is not well defined. It remains unclear whether the authors are trying to demonstrate correlation between glycosylation level and all enzymes studied in the manuscript.
Second comment is that it will be more convincing to show quantitative data to support the statement that glycosylation levels are different in benign/malignant cells.
As commented in section 'experimental design', please provide quantitative measurement of glycosylation levels in addition to the current method to support your discovery.
The causality between glycosylation and enzyme levels is weak. From this aspect, at least two more experiments need to be presented. First is the actual level of enzymes of interest by protein assay. Second is knockdown assay. Since only the overall intracellular glycosylation level has been measured, it will be very challenging to isolate related enzymes and figure out their impact. GEO data can be useful, but it is not supposed to be the most critical component of the study, you will need to add a lot more studies to support your conclusion.
All text and materials provided via this peer-review history page are made available under a Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.