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Analysis of Lysosomal Proteome Changes in Microbial Infection

Lysosomal membranes and related proteins are involved in the response to a variety of microbial infections. Therefore, elucidating the changes in lysosomal proteins upon microbial infection is of great interest and contributes to improving the understanding of lysosomal function. Here, CD BioSciences provides an effective service to analyze lysosomal proteome changes in microbial infection.

Background of Lysosomal Proteome Changes in Microbial Infection Analysis

Lysosomes are not only a degrading organelle, they are also involved in immune cells against pathogens and play a crucial role in both innate and adaptive immunity. Proteins in the lysosomal cell membrane and lumen affect its function. In particular, hydrolases and acidifying proteins are essential to guarantee proper lysosomal function under different physiological and pathological conditions such as starvation and infection. However, we currently know little about the lysosomal proteomic changes induced by various microbial infections. The autophagy-lysosome degradation pathway function is involved in the host cell defense against microbial infections. Moreover, different pathogens employ different strategies to evade lysosomal degradation. For example, Listeria monocytogenes secretes toxins that disrupt lysosomal membranes to evade phagocytosis.

Fig. 1. Proteomic analysis of Trichomonas vaginalis phagolysosome, lysosomal targeting, and unconventional secretion of cysteine peptidases. (Zimmann N, et al., 2022)Fig. 1. Proteomic analysis of Trichomonas vaginalis phagolysosome, lysosomal targeting, and unconventional secretion of cysteine peptidases. (Zimmann N, et al., 2022)

Our Lysosomal Proteome Changes in Microbial Infection Analysis Services

Microorganisms are usually cleared by phagocytosis and killed by phagosomal-lysosomal fusion. Proteomics strategies have been widely used for proteomic analysis under different cellular conditions, and mass spectrometry-based studies have revealed the critical role of lysosomal membranes and associated proteins for viral infection. Here, CD BioSciences focuses on the protein composition of lysosomes and comprehensively analyzes the changes in lysosomal protein abundance that occur in different microbial infections.

Our goal is to analyze the response and proteomic changes of intact and mature lysosomes to various types of microbial infections through an integrated proteomic strategy. Our engineers use a combination of differential and density ultracentrifugation to enrich lysosomes from cells of infected microorganisms, followed by TMT labeling and LC-MS/MS for proteomic analysis. We can analyze different types of pathogens.

  • Bacteria (Listeria monocytogenes, L. m).
  • DNA viruses (Herpes simplex virus type 1, HSV-1).
  • RNA viruses (herpes stomatitis virus, VSV).
  • Trichomonas vaginalis.

Our Advantages

  • Combination of multiple advanced techniques, bioinformatics, differential and density ultracentrifugation, TMT labeling and LC-MS/MS.
  • Identification of thousands of lysosome-associated proteins and hundreds of potential glycosylation sites.
  • Analyzes the diversity of lysosomal responses to different pathogenic infections by comparison.
  • Identifies the most significant changes in proteins and fluctuations in glycosylation at the whole cell level.
  • A protein-protein interaction network can be constructed for differentially expressed proteins.

We look forward to collaborating with you. You are always welcome to engage in discussions with us at any point of the project. If you are interested in our services, please feel free to contact us for more information.

References

  1. Xu B, Gao Y, Zhan S, et al. (2017) Quantitative proteomic profiling for clarification of the crucial roles of lysosomes in microbial infections[J]. Molecular Immunology. 87: 122-131.
  2. Zimmann N, Rada P, Žárský V, et al. (2022) Proteomic analysis of Trichomonas vaginalis phagolysosome, lysosomal targeting, and unconventional secretion of cysteine peptidases[J]. Molecular & Cellular Proteomics. 21(1).

For research use only, not intended for any clinical use.

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