Clinical Value of Glycan Changes in Cerebrospinal Fluid for Evaluation of Post-Neurosurgical Bacterial Meningitis with Hemorrhagic Stroke Patients

Abstract

Post-neurosurgical bacterial meningitis (PNBM) is one of the severe complications in patients receiving neurosurgical procedures. Recent studies have found microbe-related glycans play important roles in adhesion, invasion, and toxicity toward innate immunological reactions. In this study, we aimed to investigate the glycomic profile and its potential diagnostic efficacy in post-neurosurgical bacterial meningitis (PNBM) patients with hemorrhagic stroke. A total of 136 cerebrospinal fluid (CSF) samples were recruited and divided into a PNBM group and a non-PNBM group based on the clinical diagnostic criteria. A lectin biochip-based method was established for the detection of glycans in CSF. The clinicopathological data and biochemical parameters in CSF from all patients were analyzed. Two models for multivariate analysis investigating glycan changes in the CSF were conducted, aiming at determining the specific expression and diagnostic efficacy of lectin-probing glycans (LPGs) for PNBM. In univariate analysis, we found that 8 out of 11 LPGs were significantly correlated with PNBM. Model 1 multivariate analysis revealed that PNA (p = 0.034), Jacalin (p = 0.034) and LTL (p = 0.001) were differentially expressed in the CSF of PNBM patients compared with those of non-PNBM patients. Model 2 multivariate analysis further disclosed that LTL (p = 0.021) and CSF glucose (p < 0.001) had independent diagnostic efficacies in PNBM, with areas under the curve (AUC) of 0.703 and 0.922, respectively. In summary, this study provided a new insight into the subject of CSF glycomics concerning bacterial infection in patients with hemorrhagic stroke.

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“…After that, we labeled the samples with Cy3 following our previous method. 16 A PD Mini Trap G‐25 column (GE, Massachusetts, USA) was used to remove free Cy3 and obtain the Cy3‐labeled samples.…”

“…We carried out chemical surface modifications of the gold biochip surface according to an established protocol. 16 Lectins, including Lotus tetragonolobus lectin (LTL, L‐1320), Lens culinaris agglutinin (LCA, L‐1040), Narcissus pseudonarcissus lectin (NPL, L‐1370), Jacalin (L‐1150), Ricinus communis agglutinin I (RCA‐I, L‐1080), Peanut agglutinin (PNA, L‐1070), Vicia villosa lectin (VVL, L‐1230), Wheat germ agglutinin (WGA, L‐1020), Maackia amurensis lectin I (MAL‐I, L‐1310), Sambucus nigra lectin (SNA, L‐1300), and concanavalin A (Con A L‐1000‐500), were commercially purchased from Vector Laboratories (CA, USA). We described these lectins, which specifically bind to different glycans, in our previous study.…”

“…Thus, we obtained samples containing approximately 400 μL of filtrate without high‐abundance proteins, and we used a BCA Protein Assay Kit (Spark Jade, Shandong, China) to quantify the purified sample proteins in each of them. After that, we labeled the samples with Cy3 following our previous method 16 . A PD Mini Trap G‐25 column (GE, Massachusetts, USA) was used to remove free Cy3 and obtain the Cy3‐labeled samples.…”