Skip to main content

Thank you for visiting nature.com. You are using a browser version with limited support for CSS. To obtain the best experience, we recommend you use a more up to date browser (or turn off compatibility mode in Internet Explorer). In the meantime, to ensure continued support, we are displaying the site without styles and JavaScript.

Advertisement

Scientific Reports
  • View all journals
  • Search
  • My Account Login
  • Content Explore content
  • About the journal
  • Publish with us
  • Sign up for alerts
  • RSS feed
  1. nature
  2. scientific reports
  3. articles
  4. article
Comprehensive proteomics analysis of bovine sperm head plasma membrane associated with fertility
Download PDF
Download PDF
  • Article
  • Open access
  • Published: 03 April 2026

Comprehensive proteomics analysis of bovine sperm head plasma membrane associated with fertility

  • Muhammad Imran1,2 nAff4,
  • Mary M. Buhr1,
  • Paulos Chumala2 &
  • …
  • George S. Katselis2,3 

Scientific Reports , Article number:  (2026) Cite this article

We are providing an unedited version of this manuscript to give early access to its findings. Before final publication, the manuscript will undergo further editing. Please note there may be errors present which affect the content, and all legal disclaimers apply.

Subjects

  • Physiology
  • Zoology

Abstract

Bull fertility impacts herd fertility, but accurately predicting male fertility from sperm characteristics is difficult once extremes are removed. The objectives of this study were identification, relative quantification, and comparison of sperm head plasma membrane (HPM) proteomics in bulls of differing bull fertility index (BFI). HPM from one fresh ejaculate from 16 Holstein bulls (8 each high and low fertility) was extracted, digested and assessed by liquid chromatography-tandem mass spectrometry (LC-MS/MS). The MS spectra were aligned to UniProtKB mammals, identified, and characterized by Spectrum Mill. Mass Profiler Professional statistical analysis of the 22,117 total proteins identified in all bulls, after database search, revealed 67 proteins [unique plus homologous, 1% false discovery rate] whose abundance differed at least 2-fold (differentially abundant proteins, DAPs) between the 3 bulls each with highest and lowest BFI [high fertility (HF) BFI 105.66 ± 0.54 > low fertility (LF) BFI 91.33 ± 1.44; p < 0.01]. Gene ontology assigned the 48 DAPS increased in HF to sperm-specific function and fertility-related mechanisms, and the 19 HF-decreased DAPs primarily to catalytic and transporter activity. Meta analysis and linear regression each confirmed that the BFI of the 6 HF/LF bulls significantly correlated to the DAPS (regression r2 = 0.65 to 0.97, p ≤ 0.05), but importantly in the 16-bull population, linear regression found that 38 of the HF-increased DAPS positively correlated to BFI (r2 = 0.29 to 0.66; p ≤ 0.05), and 4 of the HF-decreased DAPS negatively correlated (r2 = 0.26 to 0.44; p ≤ 0.05). In summary, this study identified HPM proteins with important roles in sperm fertilization and significant correlations with bull fertility.

Data availability

The mass spectrometry proteomics data have been deposited to the ProteomeXchange Consortium via the PRIDE partner repository [61] with the dataset identifier PXD047294 and are available from the corresponding author on reasonable request.

Abbreviations

ACRBP:

Acrosin binding protein

ADAM:

A disintegrin and metalloproteinase

AE:

Acrosomal exocytosis

AI:

Artificial insemination

AK5:

Adenylate kinase 5

AK7:

Adenylate kinase 7

AKAP3:

A-kinase anchoring protein 3

ATL2:

Atlastin-2

ATP:

Adenosine triphosphate

ATP5D:

ATP synthase subunit d

ATP5F1:

ATP synthase F(0) complex subunit B1

ATP5H:

ATP synthase subunit d

ATP5J2:

ATP synthase subunit d

BFI:

Bull fertility index

CASA:

Computer-assisted sperm analysis

DAPs:

Differentially abundant proteins

DNAI1:

Dynein axonemal intermediate chain 1

ELSPBP1:

Epididymal sperm-binding protein 1

FDR:

False discovery rate

GO:

Gene ontology

GPX4:

Glutathione peroxidase 4

HF:

High fertility

HPM:

High-performance membrane

LC/MS:

Liquid chromatography/mass spectrometry

LC-MS/MS:

Liquid chromatography-mass spectrometry/mass spectrometry

LF:

Low fertility

LDHA:

L-lactate dehydrogenase A chain

MPP:

Mass profiler professional

MCODE:

Molecular complex detection

MS:

Mass spectrometry

ND:

No data/not detected

NME5:

Non-metastatic cells 5, protein expressing

NRR:

Non-return rate

NT5C1A:

5’-Nucleotidase, cytosolic IA

NT5C1B:

5’-Nucleotidase, cytosolic IB

OGC:

Observed gene count

ODF1:

Outer dense fiber protein 1

PATHER:

Pathway analysis through hidden entities and relationships

PCA:

Principal component analysis

PKA:

Protein kinase A

PPI:

Protein-protein interaction

RAB2A:

Ras-related protein Rab-2 A

RAB2B:

Ras-related protein Rab-2B

RIBC2:

RIB43A-like with coiled-coils protein 2

ROPN1L:

Rhophilin associated tail protein 1-like

ROS:

Reactive oxygen species

RSPH6A:

Radial spoke head component 6 homolog A

SPATA19:

Spermatogenesis-associated protein 19

STRING:

Search tool for the retrieval of interacting genes/proteins

SUCLA2:

Succinate-CoA ligase ADP-forming subunit beta

TPI1:

Triosephosphate isomerase

TPTE:

Tyrosine-protein phosphatase

UniProt:

Universal protein resource

UniProtKB:

Universal protein resource knowledgebase

ZAN:

Zonadhesin

ZPBP1:

Zona pellucida-binding protein 1

ZPBP2:

Zona pellucida-binding protein 2

References

  1. Amann, R. P., Saacke, R. G., Barbato, G. F. & Waberski, D. Measuring Male-to-Male differences in fertility or effects of semen treatments. Annu. Rev. Anim. Biosci. 6, 255–286. https://doi.org/10.1146/annurev-animal-030117-014829 (2018).

    Google Scholar 

  2. Graham, J. K. & Mocé, E. Fertility evaluation of frozen/thawed semen. Theriogenology 64, 492–504. https://doi.org/10.1016/j.theriogenology.2005.05.006 (2005).

    Google Scholar 

  3. Watson, P. F. The causes of reduced fertility with cryopreserved semen. Anim. Reprod. Sci. 60–61, 481–492. https://doi.org/10.1016/S0378-4320(00)00099-3 (2000).

    Google Scholar 

  4. D’Amours, O. et al. Proteomic markers of functional sperm population in bovines: comparison of Low- and High-Density spermatozoa following cryopreservation. J. Proteome Res. 17, 177–188. https://doi.org/10.1021/acs.jproteome.7b00493 (2018).

    Google Scholar 

  5. Butler, M. L., Bormann, J. M., Weaber, R. L., Grieger, D. M. & Rolf, M. M. Selection for bull fertility: a review. Translational Anim. Sci. 4, 423–441. https://doi.org/10.1093/tas/txz174 (2020).

    Google Scholar 

  6. Tahmasbpour, E., Balasubramanian, D. & Agarwal, A. A multi-faceted approach to Understanding male infertility: gene mutations, molecular defects and assisted reproductive techniques (ART). J. Assist. Reprod. Genet. 31, 1115–1137. https://doi.org/10.1007/s10815-014-0280-6 (2014).

    Google Scholar 

  7. Kasimanickam, R. K., Kasimanickam, V. R., Arangasamy, A. & Kastelic, J. P. Sperm and seminal plasma proteomics of high- versus low-fertility Holstein bulls. Theriogenology 126, 41–48. https://doi.org/10.1016/j.theriogenology.2018.11.032 (2019).

    Google Scholar 

  8. Sudano, M. J. et al. Use of bayesian inference to correlate in vitro embryo production and in vivo fertility in Zebu Bulls. Veterinary Medicine International. 2011, 1–6. (2011). https://doi.org/10.4061/2011/436381

  9. Peddinti, D. et al. Comprehensive proteomic analysis of bovine spermatozoa of varying fertility rates and identification of biomarkers associated with fertility. BMC Syst. Biol. 2, 19–19. https://doi.org/10.1186/1752-0509-2-19 (2008).

    Google Scholar 

  10. Kumaresan, M. K. M. A., Yadav, A., Mohanty, S., Datta, T. K. & T. K. & Comparative proteomic analysis of high- and low‐fertile Buffalo bull spermatozoa for identification of fertility‐associated proteins. Reprod. Domest. Anim. 54, 786–794. https://doi.org/10.1111/rda.13426 (2019).

    Google Scholar 

  11. Awda, B. J. et al. Existence and importance of Na(+)K(+)-ATPase in the plasma membrane of Boar spermatozoa. Can. J. Physiol. Pharmacol. https://doi.org/10.1139/cjpp-2023-0116 (2023).

    Google Scholar 

  12. Singh, R. et al. Functional proteomic analysis of crossbred (Holstein Friesian × Sahiwal) bull spermatozoa. Reprod. Domest. Anim. 53, 588–608. https://doi.org/10.1111/rda.13146 (2018).

    Google Scholar 

  13. Viana, A. G. A. et al. Proteomic landscape of seminal plasma associated with dairy bull fertility. Sci. Rep. 8, 16323–16323. https://doi.org/10.1038/s41598-018-34152-w (2018).

    Google Scholar 

  14. Somashekar, L. et al. Comparative sperm protein profiling in bulls differing in fertility and identification of phosphatidylethanolamine-binding protein 4, a potential fertility marker. Andrology 5, 1032–1051. https://doi.org/10.1111/andr.12404 (2017).

    Google Scholar 

  15. Muhammad Aslam, M. K. et al. Identification of biomarker candidates for fertility in spermatozoa of crossbred bulls through comparative proteomics. Theriogenology 119, 43–51. https://doi.org/10.1016/j.theriogenology.2018.06.021 (2018).

    Google Scholar 

  16. Byrne, K., Leahy, T., McCulloch, R., Colgrave, M. L. & Holland, M. K. Comprehensive mapping of the bull sperm surface proteome. PROTEOMICS 12, 3559–3579. https://doi.org/10.1002/pmic.201200133 (2012).

    Google Scholar 

  17. Gadella, B. M. & Boerke, A. An update on post-ejaculatory remodeling of the sperm surface before mammalian fertilization. Theriogenology 85, 113–124. https://doi.org/10.1016/j.theriogenology.2015.07.018 (2016).

    Google Scholar 

  18. Caballero, J. et al. Bovine sperm raft membrane associated glioma Pathogenesis-Related 1-like protein 1 (GliPr1L1) is modified during the epididymal transit and is potentially involved in sperm binding to the Zona pellucida. J. Cell. Physiol. 227, 3876–3886. https://doi.org/10.1002/jcp.24099 (2012).

    Google Scholar 

  19. Imran, M. Identification and Quantification of Sperm Head Plasma Membrane Proteins Associated with Male Fertility. PhD Thesis, College of Graduate and Postdoctoral Studies p. 258, University of Saskatchewan, Saskatoon, SK, Canada. (2023).

  20. Zhao, Y. & Buhr, M. M. Localization of various ATPases in fresh and cryopreserved bovine spermatozoa. Anim. Reprod. Sci. 44, 139–148. https://doi.org/10.1016/0378-4320(96)01547-3 (1996).

    Google Scholar 

  21. Mi, Y., Shi, Z. & Li, J. Spata19 is critical for sperm mitochondrial function and male fertility. Mol. Reprod. Dev. 82, 907–913. https://doi.org/10.1002/mrd.22536 (2015).

    Google Scholar 

  22. Nourashrafeddin, S., Ebrahimzadeh-Vesal, R., Modarressi, M. H., Zekri, A. & Nouri, M. Identification of Spata-19 new variant with expression beyond meiotic phase of mouse testis development. Rep. Biochem. Mol. Biology. 2, 89–93 (2014).

    Google Scholar 

  23. Lee, S., Hong, S. H. & Cho, C. Normal fertility in male mice lacking ADAM32 with testis-specific expression. Reprod. Biol. 20, 589–594. https://doi.org/10.1016/j.repbio.2020.09.001 (2020).

    Google Scholar 

  24. Munier, A. et al. A new human nm23 homologue (nm23-H5) specifically expressed in testis germinal cells. FEBS Lett. 434, 289–294. https://doi.org/10.1016/s0014-5793(98)00996-x (1998).

    Google Scholar 

  25. Zhou, J. et al. RIM-BP3 is a manchette-associated protein essential for spermiogenesis. Development 136, 373–382. https://doi.org/10.1242/dev.030858 (2009).

    Google Scholar 

  26. Teves, M. E. & Roldan, E. R. S. Sperm Bauplan and function and underlying processes of sperm formation and selection. Physiol. Rev. 102, 7–60. https://doi.org/10.1152/physrev.00009.2020 (2022).

    Google Scholar 

  27. Whitfield, M. et al. Mutations in DNAH17, encoding a Sperm-Specific axonemal outer dynein arm heavy Chain, cause isolated male infertility due to asthenozoospermia. Am. J. Hum. Genet. 105, 198–212. https://doi.org/10.1016/j.ajhg.2019.04.015 (2019).

    Google Scholar 

  28. Vignjevic, D. & Montagnac, G. Reorganisation of the dendritic actin network during cancer cell migration and invasion. Sem. Cancer Biol. 18, 12–22. https://doi.org/10.1016/j.semcancer.2007.08.001 (2008).

    Google Scholar 

  29. Austin, C. R. The ‘Capacitation’ of the mammalian sperm. Nature 170, 326–326. https://doi.org/10.1038/170326a0 (1952).

    Google Scholar 

  30. Petit, F. M., Serres, C., Bourgeon, F., Pineau, C. & Auer, J. Identification of sperm head proteins involved in Zona pellucida binding. Hum. Reprod. 28, 852–865. https://doi.org/10.1093/humrep/des452 (2013).

    Google Scholar 

  31. Chen, H. et al. A testis-specific gene, TPTE, encodes a putative transmembrane tyrosine phosphatase and maps to the pericentromeric region of human chromosomes 21 and 13, and to chromosomes 15, 22, and Y. Hum. Genet. 105, 399–409. https://doi.org/10.1007/s004399900144 (1999).

    Google Scholar 

  32. Tükenmez, H., Magnussen, H. M., Kovermann, M., Byström, A. & Wolf-Watz, M. Linkage between fitness of yeast cells and adenylate kinase catalysis. PLOS ONE. 11, e0163115–e0163115. https://doi.org/10.1371/journal.pone.0163115 (2016).

    Google Scholar 

  33. Yu, J. et al. ATP synthase is required for male fertility and germ cell maturation in drosophila testes. Mol. Med. Rep. https://doi.org/10.3892/mmr.2019.9834 (2019).

    Google Scholar 

  34. Rajamanickam, G. D., Kastelic, J. P. & Thundathil, J. C. Content of testis-specific isoform of Na/K-ATPase (ATP1A4) is increased during bovine sperm capacitation through translation in mitochondrial ribosomes. Cell Tissue Res. 368, 187–200. https://doi.org/10.1007/s00441-016-2514-7 (2017).

    Google Scholar 

  35. Chen, J. et al. Functional expression of Ropporin in human testis and ejaculated spermatozoa. J. Androl. 32, 26–32. https://doi.org/10.2164/jandrol.109.009662 (2011).

    Google Scholar 

  36. Zhao, W. et al. Outer dense fibers stabilize the axoneme to maintain sperm motility. J. Cell. Mol. Med. 22, 1755–1768. https://doi.org/10.1111/jcmm.13457 (2018).

    Google Scholar 

  37. Xu, K., Yang, L., Zhang, L. & Qi, H. Lack of AKAP3 disrupts integrity of the subcellular structure and proteome of mouse sperm and causes male sterility. Development 147 https://doi.org/10.1242/dev.181057 (2020).

  38. Li, Y. F. et al. CABYR binds to AKAP3 and Ropporin in the human sperm fibrous sheath. Asian J. Androl. 13, 266–274. https://doi.org/10.1038/aja.2010.149 (2011).

    Google Scholar 

  39. Martin-Hidalgo, D., Macias-Garcia, B., Garcia-Marin, L. J., Bragado, M. J. & Gonzalez-Fernandez, L. Boar spermatozoa proteomic profile varies in sperm collected during the summer and winter. Anim. Reprod. Sci. 219, 106513. https://doi.org/10.1016/j.anireprosci.2020.106513 (2020).

    Google Scholar 

  40. Bechtel, S. et al. The full-ORF clone resource of the German cDNA consortium. BMC Genom. 8, 399. https://doi.org/10.1186/1471-2164-8-399 (2007).

    Google Scholar 

  41. Lin, Y. H. et al. RAB10 interacts with the male germ Cell-Specific GTPase-Activating protein during mammalian spermiogenesis. Int. J. Mol. Sci. 18, 97–97. https://doi.org/10.3390/ijms18010097 (2017).

    Google Scholar 

  42. Torra-Massana, M. et al. Altered mitochondrial function in spermatozoa from patients with repetitive fertilization failure after ICSI revealed by proteomics. Andrology 9, 1192–1204. https://doi.org/10.1111/andr.12991 (2021).

    Google Scholar 

  43. Mountjoy, J. R., Xu, W., McLeod, D., Hyndman, D. & Oko, R. RAB2A: A major subacrosomal protein of bovine spermatozoa implicated in acrosomal Biogenesis1. Biol. Reprod. 79, 223–232. https://doi.org/10.1095/biolreprod.107.065060 (2008).

    Google Scholar 

  44. Nassari, S., Del Olmo, T. & Jean, S. Rabs in signaling and embryonic development. Int. J. Mol. Sci. 21, 1064–1064. https://doi.org/10.3390/ijms21031064 (2020).

    Google Scholar 

  45. Stenmark, H. Rab GTPases as coordinators of vesicle traffic. Nat. Rev. Mol. Cell Biol. 10, 513–525. https://doi.org/10.1038/nrm2728 (2009).

    Google Scholar 

  46. Cho, E. H. et al. A nonsense variant in NME5 causes human primary ciliary dyskinesia with radial spoke defects. Clin. Genet. 98, 64–68. https://doi.org/10.1111/cge.13742 (2020).

    Google Scholar 

  47. Awda, B. J. & Buhr, M. M. Extracellular Signal-Regulated kinases (ERKs) pathway and reactive oxygen species regulate tyrosine phosphorylation in capacitating Boar Spermatozoa1. Biol. Reprod. 83, 750–758. https://doi.org/10.1095/biolreprod.109.082008 (2010).

    Google Scholar 

  48. Özbek, M., Hitit, M., Kaya, A., Jousan, F. D. & Memili, E. Sperm functional genome associated with bull fertility. Front. Veterinary Sci. https://doi.org/10.3389/fvets.2021.610888 (2021). 8.

    Google Scholar 

  49. Maiorino, M. et al. Functional interaction of phospholipid hydroperoxide glutathione peroxidase with sperm Mitochondrion-associated cysteine-rich protein discloses the adjacent cysteine motif as a new substrate of the selenoperoxidase. J. Biol. Chem. 280, 38395–38402. https://doi.org/10.1074/jbc.M505983200 (2005).

    Google Scholar 

  50. Rahman, M. S., Lee, J. S., Kwon, W. S. & Pang, M. G. Sperm Proteomics: Road to Male Fertility and Contraception. International Journal of Endocrinology. 2013, 1–11. (2013). https://doi.org/10.1155/2013/360986

  51. Goldberg, E. The sperm-specific form of lactate dehydrogenase is required for fertility and is an attractive target for male contraception (a review). Biol. Reprod. 104, 521–526. https://doi.org/10.1093/biolre/ioaa217 (2021).

    Google Scholar 

  52. Lin, Y. N., Roy, A., Yan, W., Burns, K. H. & Matzuk, M. M. Loss of Zona pellucida binding proteins in the acrosomal matrix disrupts acrosome biogenesis and sperm morphogenesis. Mol. Cell. Biol. 27, 6794–6805. https://doi.org/10.1128/MCB.01029-07 (2007).

    Google Scholar 

  53. Ferrer, M., Cornwall, G. & Oko, R. A population of CRES resides in the outer dense fibers of Spermatozoa1. Biol. Reprod. 88 https://doi.org/10.1095/biolreprod.112.104745 (2013).

  54. Buhr, M. M., Curtis, E. F., Thompson, J. A., Wilton, J. W. & Johnson, W. H. Diet and breed influence the sperm membranes of beef bulls. Theriogenology 39, 581–592. https://doi.org/10.1016/0093-691x(93)90245-z (1993).

    Google Scholar 

  55. Hickey, K. D. & Buhr, M. M. Characterization of Na + K+-ATPase in bovine sperm. Theriogenology 77, 1369–1380. https://doi.org/10.1016/j.theriogenology.2011.10.045 (2012).

    Google Scholar 

  56. Nair, M. et al. Lipopolysaccharides induce a RAGE-mediated sensitization of sensory neurons and fluid hypersecretion in the upper airways. Sci. Rep. 11, 8336–8336. https://doi.org/10.1038/s41598-021-86069-6 (2021).

    Google Scholar 

  57. Koziy, R. V. et al. Discovery proteomics for the detection of putative markers for eradication of infection in an experimental model of equine septic arthritis using LC-MS/MS. J. Proteom. 261, 104571–104571. https://doi.org/10.1016/j.jprot.2022.104571 (2022).

    Google Scholar 

  58. Mirzaei, H. & Regnier, F. Enrichment of carbonylated peptides using Girard P reagent and strong cation exchange chromatography. Anal. Chem. 78, 770–778. https://doi.org/10.1021/ac0514220 (2006).

    Google Scholar 

  59. Creese, A. J., Shimwell, N. J., Larkins, K. P. B., Heath, J. K. & Cooper, H. J. Probing the complementarity of FAIMS and strong cation exchange chromatography in shotgun proteomics. J. Am. Soc. Mass. Spectrom. 24, 431–443. https://doi.org/10.1007/s13361-012-0544-2 (2013).

    Google Scholar 

  60. Henry, M., Coleman, O., Prashant, Clynes, M. & Meleady, P. Phosphopeptide Enrichment and LC-MS/MS Analysis To Study the Phosphoproteome of Recombinant Chinese Hamster Ovary Cells Vol. 1603, 195–208 (Clifton, 2017). Methods in molecular biology. https://doi.org/10.1007/978-1-4939-6972-2_13

  61. Vizcaino, J. A. et al. The proteomics identifications (PRIDE) database and associated tools: status in 2013. Nucleic Acids Res. 41, D1063–1069. https://doi.org/10.1093/nar/gks1262 (2013).

    Google Scholar 

Download references

Acknowledgements

Research reported in this publication was supported by NSERC for funding and Semex in Guelph Ontario provided gift of semen and bull fertility analysis. Canadian Centre for Rural and Agricultural Health provided Founding Chairs Fellowship award to the first author and support for the MS instrumentation.

Author information

Author notes

  1. Muhammad Imran

    Present address: Department of Obstetrics & Gynecology, Faculty of Medicine and Dentistry, The Metabolomics Innovation Centre, Women and Children’s Health Research Institute, University of Alberta, Edmonton, AB, T5G 0B6, Canada

Authors and Affiliations

  1. Department of Animal and Poultry Science, College of Agriculture and Bioresources, University of Saskatchewan, 51 Campus Drive, Saskatoon, SK, S7N 5A8, Canada

    Muhammad Imran & Mary M. Buhr

  2. Canadian Centre for Rural and Agricultural Health, University of Saskatchewan, 104 Clinic Place, Saskatoon, SK, S7N 2Z4, Canada

    Muhammad Imran, Paulos Chumala & George S. Katselis

  3. Department of Medicine, College of Medicine, University of Saskatchewan, 104 Clinic Place, Saskatoon, SK, S7N 2Z4, Canada

    George S. Katselis

Authors
  1. Muhammad Imran
    View author publications

    Search author on:PubMed Google Scholar

  2. Mary M. Buhr
    View author publications

    Search author on:PubMed Google Scholar

  3. Paulos Chumala
    View author publications

    Search author on:PubMed Google Scholar

  4. George S. Katselis
    View author publications

    Search author on:PubMed Google Scholar

Contributions

Muhammad Imran: contributed to conceptualization, experimental design, conducted the study, performed data analysis, validation, visualization, wrote first draft of manuscript and revised. Mary M. Buhr: contributed to conceptualization, funding acquisition, project administration, resources, supervision and manuscript revision and final approval. Paulos Chumala: contributed to acquiring MS data and data analysis. George S. Katselis: contributed to conceptualization of the experimental design, funding acquisition, project administration, supervision, resources and manuscript revision and final approval.

Corresponding author

Correspondence to George S. Katselis.

Ethics declarations

Competing interests

The authors declare no competing interests.

Additional information

Publisher’s note

Springer Nature remains neutral with regard to jurisdictional claims in published maps and institutional affiliations.

Rights and permissions

Open Access This article is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License, which permits any non-commercial use, sharing, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if you modified the licensed material. You do not have permission under this licence to share adapted material derived from this article or parts of it. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by-nc-nd/4.0/.

Reprints and permissions

About this article

Check for updates. Verify currency and authenticity via CrossMark

Cite this article

Imran, M., Buhr, M.M., Chumala, P. et al. Comprehensive proteomics analysis of bovine sperm head plasma membrane associated with fertility. Sci Rep (2026). https://doi.org/10.1038/s41598-025-34626-8

Download citation

  • Received: 30 June 2025

  • Accepted: 30 December 2025

  • Published: 03 April 2026

  • DOI: https://doi.org/10.1038/s41598-025-34626-8

Share this article

Anyone you share the following link with will be able to read this content:

Sorry, a shareable link is not currently available for this article.

Provided by the Springer Nature SharedIt content-sharing initiative

Keywords

  • Fertilization
  • Predicting bull fertility
  • Sperm HPM
  • Fertility biomarkers
  • Mass spectrometry-based proteomics
Download PDF

Advertisement

Explore content

  • Research articles
  • News & Comment
  • Collections
  • Subjects
  • Follow us on Facebook
  • Follow us on X
  • Sign up for alerts
  • RSS feed

About the journal

  • About Scientific Reports
  • Contact
  • Journal policies
  • Guide to referees
  • Calls for Papers
  • Editor's Choice
  • Journal highlights
  • Open Access Fees and Funding

Publish with us

  • For authors
  • Language editing services
  • Open access funding
  • Submit manuscript

Search

Advanced search

Quick links

  • Explore articles by subject
  • Find a job
  • Guide to authors
  • Editorial policies

Scientific Reports (Sci Rep)

ISSN 2045-2322 (online)

nature.com footer links

About Nature Portfolio

  • About us
  • Press releases
  • Press office
  • Contact us

Discover content

  • Journals A-Z
  • Articles by subject
  • protocols.io
  • Nature Index

Publishing policies

  • Nature portfolio policies
  • Open access

Author & Researcher services

  • Reprints & permissions
  • Research data
  • Language editing
  • Scientific editing
  • Nature Masterclasses
  • Research Solutions

Libraries & institutions

  • Librarian service & tools
  • Librarian portal
  • Open research
  • Recommend to library

Advertising & partnerships

  • Advertising
  • Partnerships & Services
  • Media kits
  • Branded content

Professional development

  • Nature Awards
  • Nature Careers
  • Nature Conferences

Regional websites

  • Nature Africa
  • Nature China
  • Nature India
  • Nature Japan
  • Nature Middle East
  • Privacy Policy
  • Use of cookies
  • Legal notice
  • Accessibility statement
  • Terms & Conditions
  • Your US state privacy rights
Springer Nature

© 2026 Springer Nature Limited

Nature Briefing

Sign up for the Nature Briefing newsletter — what matters in science, free to your inbox daily.

Get the most important science stories of the day, free in your inbox. Sign up for Nature Briefing