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ST

streptokinase (Shankinase)

✓ Approved

Sanofi S.A · PLG · Recombinant Proteins

What is streptokinase?

streptokinase is a recombinant proteins developed by Sanofi S.A. It is approved for therapeutic indications via injectable (others) or intravenous (iv).

Drug Profile

Brand NamesShankinase
CompanySanofi S.A
Drug ClassRecombinant Proteins
Molecular TargetPLG
RouteInjectable (Others), Intravenous (IV)
StatusApproved
Sources: ClinicalTrials.gov, Sanofi S.A

Mechanism of Action

Molecular Targets

streptokinase acts on 1 molecular target:

PLGplasminogen (HAE4)
Want deeper analysis?Noah AI can explain complex mechanisms and compare to similar drugs.

Therapeutic Indications

streptokinase is developed for 4 unique indications across 3 therapeutic areas.

Therapeutic AreaConditionPhase
Vascular disordersArterial thrombosis✓ Approved
Cardiac disordersMyocardial infarction✓ Approved
Respiratory, thoracic and mediastinal disordersPulmonary thrombosis✓ Approved
Vascular disordersVenous thrombosis✓ Approved

Related Research Articles

PubMedPakistan journal of medical sciences2026-10-01

Outcomes of thrombolytic therapy in prosthetic valve thrombosis; a single centre study.

Rana Ikram Ahmed IA, Munawar Fatina F, Mubasher Ayesha A, Talha Bajwa Muhammad M

To determine the outcomes of thrombolytic therapy in prosthetic valve thrombosis. Data was taken from the hospital discharge database, of the Tahir Heart Institute, for patients admitted from January 01, 2016 to June 30, 2024. Definitive diagnosis was made with transthoracic echocardiography showing an obstructed prosthetic valve for patients presenting with new-onset dyspnea. Streptokinase infusion was given per ACC/AHA guidelines with twelve-hourly TTE for transvalvular gradient assessment. The primary outcome was successful thrombolysis with reduction in transvalvular gradients. Data was analyzed by Microsoft Excel. Patients were followed up over time. Approximately 0.1% of total hospital admissions, i.e. twenty-seven cases, were found to have prosthetic valve thrombosis. Target gradients on TTE were achieved for 71% (n=17) of mitral and 100% (n=3) of aortic valves: thrombolysis was successful in 74% (n=20), partial success in 18.5% (n=5) and unsuccessful in 7.4% (n=2) of cases. Subsequent complications were: myocardial infarction 7.4% (n=2), embolic phenomena 14.8 % (n=4), coronary emboli 7.4% (n=2), brain emboli 7.4% (n=2), re-thromboses 7.4% (n=2) and in-hospital mortality 7.4% (n=2) of cases. The mean time for follow-up after discharge was 3.04 ± 2.07 years; one patient died a year after discharge. Thrombolytic therapy with streptokinase has been shown to be an effective and relatively safe method for managing prosthetic valve thrombosis.

PMID 42819587
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PubMedHuman immunology2026-09-29

Rational truncation of streptokinase reduces immunogenicity while preserving plasminogen activation: in vitro and in vivo analysis.

Gunasekaran Vijay V, Suthakaran Pichaimuthu P, Namasivayam Vigneshwaran V, Ponnusami V V

The clinical utility of streptokinase, a widely used and cost-effective thrombolytic agent, has gained importance post COVID-19 due to increase in cardiovascular diseases globally. But the strong humoral immunogenicity exhibited by it, restricts its usage. Building upon our prior work of developing truncated streptokinase variants and their plasminogen activation study, we report here the results of immunogenicity studies for identification of variants with reduced immunogenicity. A panel of ten rationally truncated and recombinantly expressed streptokinase fragments were screened for antibody recognition and immunogenicity potential. Out of the ten fragments, two N-terminal constructs (amino acid residues 1-300 and 1-173) exhibited approximately 40-45% lower ELISA immunoreactivity compared with full-length streptokinase during initial in vitro screening. These fragments were also already reported to retain >85% of native plasminogen activation activity. In vivo evaluation of the fragments in rabbits demonstrated significantly attenuated humoral responses over a 28-day immunization period, confirmed by longitudinal antibody titration and cumulative area-under-the-curve analysis when compared to the full-length streptokinase. Fragment 1-173 emerged as a promising lower-immunogenic thrombolytic candidate, and this work demonstrates that rational domain minimization can decouple functional competence from immunodominant regions in streptokinase establishing a broadly applicable framework for engineering improved therapeutic proteins.

PMID 42810275
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PubMedJournal of structural biology2026-09-24

In silico engineering fibrin-directed streptokinase - kringle 2 fusion: Structural insights into fibrin interaction and plasminogen recognition.

Mohammed Rawaa Kh RK, Buniya Harith K HK

Streptokinase (SK) is an effective plasminogen-activating fibrinolytic protein, but its lack of intrinsic fibrin specificity limits thrombus-directed fibrinolysis. We computationally evaluated an engineered SK-K2 fusion in which the fibrin-interacting Kringle 2 (K2) domain of human tissue-type plasminogen activator was appended to the SK C-terminus. Structural modeling showed high K2 confidence (mean pLDDT = 85.67), and all 22 K2 residues at the predicted fibrin interface had pLDDT values ≥70 (mean = 89.88). HDOCK ranked SK-K2-fibrin more favorably than native SK-fibrin (-276.71 vs. -249.24), while PRODIGY predicted a more favorable binding free energy (-14.9 vs. -13.3 kcal/mol). Although native SK showed a more favorable HDOCK score toward plasminogen, both plasminogen complexes had identical PRODIGY-predicted binding free energies (-11.2 kcal/mol) and closely comparable dissociation constants, indicating no marked computational loss in predicted plasminogen-binding characteristics after K2 fusion. PDBePISA showed direct K2 participation and a larger chain-matched fibrin interface for SK-K2 than native SK, with six hydrogen bonds and an Asp291-Arg515 salt bridge (2.966 Å) in the HDOCK-derived complex. An independent MOE workflow reproduced the fibrin-directed ranking, with SK-K2 showing a more favorable S score than native SK (-101.8501 vs. -93.9472). PDBePISA analysis of the independent MOE complex identified Arg515 in a second salt bridge, Arg515-Glu220 (3.369 Å), providing residue-level convergence across both docking models. These findings support the structural rationale for C-terminal K2 engineering of SK and prioritize SK-K2, particularly Arg515, for experimental evaluation of fibrin association, plasminogen activation, and clot-directed fibrinolysis.

PMID 42785651
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PubMedActa cirurgica brasileira2026-09-17

Evaluation of polymeric films and streptokinase for prevention of postoperative intra-abdominal adhesion in rabbits.

Teixeira Luisa Gouvêa LG, Brito Helena Cristina Delgado HCD, Teixeira Bruna Nunes BN, Barata Julielton de Souza JS et al.

To evaluate the effectiveness of polymer-based strategies for preventing intra-abdominal adhesions after small colon enterotomy and enterorrhaphy in a rabbit experimental model. Twenty-four female New Zealand White rabbits were randomly allocated into four groups (n = 6): film composed of a blend of sodium carboxymethylcellulose and polyvinyl alcohol (NaCMC-PVA); NaCMC-PVA-streptokinase (STP) film; intra-abdominal STP infusion; and no treatment. Hematological parameters were assessed preoperatively and at three and seven days postoperatively. Macroscopic evaluation of intra-abdominal adhesions and histopathological analysis of the enterorrhaphy site were performed on postoperative day 7. Results were compared within and between experimental groups. Treated groups exhibited fewer hematological alterations compared with the control group. No statistically significant differences were observed among groups regarding adhesion severity or histopathological scores (p> 0.05). The NaCMC-PVA film showed the lowest absolute incidence of adhesions and did not impair intestinal remesothelialization. Based on the biological findings from this study, the NaCMC-PVA film exhibited acceptable handling characteristics and biological compatibility. These findings suggest its potential as a mechanical barrier for preventing abdominal adhesion. However, further studies with larger sample sizes and longer follow-up periods are required to confirm its effectiveness.

PMID 42752722
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PubMedCirculation reports2026-09-11

Development and External Validation of a Machine Learning-Based Bleeding Risk Score for Patients Undergoing Percutaneous Coronary Intervention.

Tokai Tatsuya T, Ishii Masanobu M, Ikebe So S, Nakamura Taishi T et al.

Conventional bleeding risk scores after percutaneous coronary intervention (PCI) have limited discrimination and external validation, so we developed and validated a machine learning (ML)-based bleeding risk score using real-world data. The primary outcome was major bleeding. In the Clinical Deep Data Accumulation System (CLIDAS) cohort, bleeding events occurring >30 days after PCI were identified by chart review and classified as moderate or severe bleeding by the Global Utilization of Streptokinase and TPA for Occluded Coronary Arteries criteria. In the Health, Clinic, and Education Information Evaluation Institute (HCEI) cohort, major bleeding was identified using ICD-10 codes and Diagnosis Procedure Combination (DPC) data. We analyzed 2,502 acute coronary syndrome patients undergoing PCI from CLIDAS and externally validated the model in 10,928 patients from HCEI. A total of 5 ML algorithms were trained. Key predictors were age, body mass index, Btype natriuretic peptide, and hemoglobin. Logistic regression demonstrated the best performance (area under the curve [AUC] 0.748) and was used to derive the CLIDAS bleeding risk score. The CLIDAS score outperformed the binary J-HBR (AUC 0.74 vs. 0.63, P=0.007) and binary ARC-HBR (AUC 0.74 vs. 0.62, P=0.011), but in external validation the CLIDAS score demonstrated limited discrimination (AUC 0.64), lower than continuous conventional scores. Our novel ML-based bleeding risk score showed better discrimination than conventional binary classifications in the derivation/internal validation, but external performance was limited.

PMID 42724133
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PubMedJournal of thrombosis and haemostasis : JTH2026-09-08

Mapping the mutational landscape for streptokinase binding to plasminogen.

Baid Srishti S, Holding Matthew L ML, Laurin Taylor T, Siemieniak David D et al.

Group A Streptococcus (GAS) expresses streptokinase (SK), a critical virulence factor that nonenzymatically activates the host's plasminogen (PLG) to an active form (PLGSK) via a conformational change. PLGSK then activates PLG to plasmin, resulting in fibrinolysis and facilitating bacterial dissemination. As a potent thrombolytic, SK has been used as a therapeutic agent. GAS SK is highly specific for human PLG, and sequence variation among SKs from different GAS strains has been linked to differences in PLG binding and disease severity. The contributions of individual amino acids to these differences remain poorly understood. We used phage display and deep mutational scanning to map how amino acid substitutions in SK from Group C Streptococcus (GCS), which shares high sequence homology with GAS, affect its ability to bind human PLG. We demonstrate that SK, expressed as a fusion protein with the p3 coat protein of the M13 filamentous phage, retains its ability to bind human PLG. Deep mutational scanning mapped 71% of all possible single amino acid substitutions within SK, identifying specific regions where substitutions are likely to increase or decrease its affinity for PLG. Our findings suggest a complex protein-protein interaction in which long-range protein dynamics influence the conformational activation of PLG to PLGSK. These data lay the foundation for linking SK variation across GCS strains to differences in virulence, mapping the determinants of GCS SK's human specificity, and potentially contributing to the development of improved therapeutics for heart attack and stroke.

PMID 42710811
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