ResearchSpace :: Browsing by Author "Tsekoa, Tsepo L"

Browsing by Author "Tsekoa, Tsepo L"

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Characterization, modelling and docking studies of Plasmodium falciparum kinase PfCDPK4
(AOSIS, 2019-04) Makungo, T; Tsekoa, Tsepo L; Theron, Anjo; Mancama, Dalubuhle T; Van Ree, T
Characterization, modelling and docking studies of Plasmodium falciparum kinase PfCDPK4: The increasing incidence of Plasmodium strains that are resistant to current frontline antimalarial drugs has become one of the greatest challenges of controlling malaria incidence and mortality. There is, therefore, an urgent need to develop novel targets and antimalarial drugs that are effective against drug-resistant malarial parasites. At the same time the need to develop antimalarial drugs that furthermore prevent disease transmission, has become an increasingly important consideration. Calcium dependent protein kinases (CDPKs) regulate a variety of biological processes in the malaria parasite Plasmodium falciparum, CDPK4 being of prime importance in Plasmodium biology. In this study the structure of PfCDPK4 was used as a template in the discovery of malaria drug leads. The model structure of PfCDPK4 was generated by homology modelling, and model validation confirmed that the model of PfCDPK4 is of stereochemical quality. The molecular modelling approach of in silico screening against the target molecule PfCDPK4 utilized a large library of chemical compounds, some natural chemical compounds, and clinically approved kinase inhibitors. In silico screening of the Biofocus library against PfCDPK4 resulted in twenty-six compounds being identified; in vitro screening confirmed that three of these compounds exhibit moderate antimalarial activity against the NF54 strain of Plasmodium falciparum, with the percentage inhibition ranging between 42% and 47%.
Characterization, modelling and docking studies of Plasmodium falciparum kinase PfCDPK4
(AOSIS, 2019-04) Makungo, T; Tsekoa, Tsepo L; Theron, Anjo; Mancama, Dalubuhle T; Van Ree, T
Characterization, modelling and docking studies of Plasmodium falciparum kinase PfCDPK4: The increasing incidence of Plasmodium strains that are resistant to current frontline antimalarial drugs has become one of the greatest challenges of controlling malaria incidence and mortality. There is, therefore, an urgent need to develop novel targets and antimalarial drugs that are effective against drug-resistant malarial parasites. At the same time the need to develop antimalarial drugs that furthermore prevent disease transmission, has become an increasingly important consideration. Calcium dependent protein kinases (CDPKs) regulate a variety of biological processes in the malaria parasite Plasmodium falciparum, CDPK4 being of prime importance in Plasmodium biology. In this study the structure of PfCDPK4 was used as a template in the discovery of malaria drug leads. The model structure of PfCDPK4 was generated by homology modelling, and model validation confirmed that the model of PfCDPK4 is of stereochemical quality. The molecular modelling approach of in silico screening against the target molecule PfCDPK4 utilized a large library of chemical compounds, some natural chemical compounds, and clinically approved kinase inhibitors. In silico screening of the Biofocus library against PfCDPK4 resulted in twenty-six compounds being identified; in vitro screening confirmed that three of these compounds exhibit moderate antimalarial activity against the NF54 strain of Plasmodium falciparum, with the percentage inhibition ranging between 42% and 47%.
Co-expression of sulphydryl oxidase and protein disulphide isomerase in Escherichia coli allows for production of soluble CRM197
(Wiley, 2017-04) Roth, Robyn L; Van Zyl, Petrus J; Tsekoa, Tsepo L; Stoychev, Stoyan H; Mamputha, Sipho; Buthelezi, Sindisiwe G; Crampton, Michael C
The aim of this article is to investigate the production of soluble cross-reacting material 197 (CRM(sub197)) in Escherichia coli, a safe and effective T-cell-dependent protein carrier for polysaccharides used in the manufacture and application of multivalent conjugate vaccines.
Efficient in vitro and in vivo activity of glyco-engineered plant-produced rabies monoclonal antibodies E559 and 62-71-3
(PLoS ONE, 2016-07) Tsekoa, Tsepo L; Lotter-Stark, Therese; Buthelezi, Sindisiwe G; Chakauya, Ereck; Stoychev, Stoyan H; Chikwamba, Rachel K
Rabies is a neglected zoonotic disease that has no effective treatment after onset of illness. However the disease can be prevented effectively by prompt administration of post exposure prophylaxis which includes administration of passive immunizing antibodies (Rabies Immune Globulin, RIG). Currently, human RIG suffers from many restrictions including limited availability, batch-to batch inconsistencies and potential for contamination with bloodborne pathogens. Anti-rabies monoclonal antibodies (mAbs) have been identified as a promising alternative to RIG. Here, we applied a plant-based transient expression system to achieve rapid, high level production and efficacy of the two highly potent anti-rabies mAbs E559 and 62-71-3. Expression levels of up to 490 mg/kg of recombinant mAbs were obtained in Nicotiana benthamiana glycosylation mutants by using a viral based transient expression system. The plant-made E559 and 62-71-3, carrying human-type fucose-free Nglycans, assembled properly and were structurally sound as determined by mass spectrometry and calorimetric density measurements. Both mAbs efficiently neutralised diverse rabies virus variants in vitro. Importantly, E559 and 62-71-3 exhibited enhanced protection against rabies virus compared to human RIG in a hamster model post-exposure challenge trial. Collectively, our results provide the basis for the development of a multi-mAb based alternative to RIG.
Enabling local production of biopharmaceuticals in South Africa
(CSIR, 2017-10) Tsekoa, Tsepo L
This presentation discusses the CSIR biopharmaceutical platforms in response to national health priorities and strategic context. Several CSIR-engineered biopharmaceutical case studies are highlighted.
Engineering approaches in plant molecular farming for global health
(2021-11) Singh, Advaita A; Pillay, Priyen; Tsekoa, Tsepo L
Since the demonstration of the first plant-produced proteins of medical interest, there has been significant growth and interest in the field of plant molecular farming, with plants now being considered a viable production platform for vaccines. Despite this interest and development by a few biopharmaceutical companies, plant molecular farming is yet to be embraced by 'big pharma'. The plant system offers a faster alternative, which is a potentially more cost-effective and scalable platform for the mass production of highly complex protein vaccines, owing to the high degree of similarity between the plant and mammalian secretory pathway. Here, we identify and address bottlenecks in the use of plants for vaccine manufacturing and discuss engineering approaches that demonstrate both the utility and versatility of the plant production system as a viable biomanufacturing platform for global health. Strategies for improving the yields and quality of plant-produced vaccines, as well as the incorporation of authentic posttranslational modifications that are essential to the functionality of these highly complex protein vaccines, will also be discussed. Case-by-case examples are considered for improving the production of functional protein-based vaccines. The combination of all these strategies provides a basis for the use of cutting-edge genome editing technology to create a general plant chassis with reduced host cell proteins, which is optimised for high-level protein production of vaccines with the correct posttranslational modifications.
Exploring viral diversity in a unique South African soil habitat
(Nature Publishing Group, 2018-01) Segobola, J; Adriaenssens, E; Tsekoa, Tsepo L; Rashamuse, Konanani; Cowan, D
The Kogelberg Biosphere Reserve in the Cape Floral Kingdom in South Africa is known for its unique plant biodiversity. The potential presence of unique microbial and viral biodiversity associated with this unique plant biodiversity led us to explore the fynbos soil using metaviromic techniques. In this study, metaviromes of a soil community from the Kogelberg Biosphere Reserve has been characterised in detail for the first time. Metaviromic DNA was recovered from soil and sequenced by Next Generation Sequencing. The MetaVir, MG-RAST and VIROME bioinformatics pipelines were used to analyse taxonomic composition, phylogenetic and functional assessments of the sequences. Taxonomic composition revealed members of the order Caudovirales, in particular the family Siphoviridae, as prevalent in the soil samples and other compared viromes. Functional analysis and other metaviromes showed a relatively high frequency of phage-related and structural proteins. Phylogenetic analysis of PolB, PolB2, terL and T7gp17 genes indicated that many viral sequences are closely related to the order Caudovirales, while the remainder were distinct from known isolates. The use of single virome which only includes double stranded DNA viruses limits this study. Novel phage sequences were detected, presenting an opportunity for future studies aimed at targeting novel genetic resources for applied biotechnology.
Functional characterisation of a metagenome derived family VIII esterase with a deacetylation activity on ß-lactam antibiotics
(Elsevier, 2013-08) Mokoena, N; Mathiba, K; Tsekoa, Tsepo L; Steenkamp, P; Rashamuse, K
Family VIII esterases represent a poorly characterised esterase family, with high sequence identity to class C b-lactamases, peptidases and penicillin binding protein. In this study we report on the metagenomic screening and biochemical characterisation of a novel esterase (Est22) derived from an acidic Leachate environment. The enzyme is 423 amino acids in length and contained 22aa signal peptide. Analysis of the Est22 primary structure revealed the presence of N-terminus S-x-x-K sequence, which is highly conserved in class C ß-lactamases, peptidases as well as carboxylesterases belonging to family VIII. Phylogenetic analysis using representative sequences from class C ß-lactamases and family VIII esterases indicated that Est22 clustered mainly with family VIII esterases. Substrate specificity profiling using p-nitrophenyl esters (C2-16) indicated that Est22 preferred shorter chain p-nitrophenyl esters (C2-C5), a characteristic typical of true carboxylesterase. In addition of hydrolysing nitrocefin, Est22 also hydrolysed first generation cephalosporin derivatives. Detailed selectivity study using cephalosporin revealed that Est22 selectively hydrolyse the ester bond of a cephalosporin derivatives leaving the amide bond of the ß-lactam ring intact. The selective nature of Est22 makes this enzyme potential candidate for use in the synthesis and modification cephalosporin based molecules.
Gel and gel-free approaches for the quantitative characterisation of complex protein mixtures
(2012-10) Buthelezi, Sindisiwe G; Tsekoa, Tsepo L; Stoychev, Stoyan H; Mancama, Dalubuhle T; Blackburn, J
The research aims to establish a reliable set of methods for profiling proteins in a complex mixture in order to allow for the mining of low abundant species.
Molecular modelling of calcium dependent protein kinase 4 (CDPK4) from Plasmodium falciparum
(Association for Computing Machinery (ACM), 2009-10) Tsekoa, Tsepo L
Malaria continues to be one of the most serious global health challenges. The increasing incidence of drug resistant Plasmodium strains has emphasised the need for urgent action in the development of new therapeutic strategies against this disease. Development of new drug targets is of vital importance in this regard. The recent availability of genomic information and the resultant observation that in many instances, protein kinases from parasitic protozoa are phylogenetically distant from those in humans has established this group of enzymes as potential drug targets in the Malaria parasite. In order to rationally design novel inhibitors and chemical tools exclusively targeting CDPKs, reliable molecular structures are needed. Structural Bioinformatics, specifically molecular modelling, can contribute immensely to improving access to structural information for these challenging targets. Here, a three dimensional structure of PfCDPK4 created by homology modelling is reported. Further, a model structure with computationally docked ATP is created. These structures will be used to facilitate the discovery and development of novel inhibitors and chemical proteomics tools for the study of this sub-family of proteins.
Molecular Modelling of Calcium Dependent Protein Kinase 4 (CDPK4) from Plasmodium falciparum
(2012-07) Tsekoa, Tsepo L; Makungo, T; Mancama, Dalubuhle T
Malaria continues to be one of the most serious global health challenges. The increasing incidence of drug resistant Plasmodium strains has emphasised the need for urgent action in the development of new therapeutic strategies against this disease. Development of new drug targets is of vital importance in this regard. The recent availability of genomic information and the resultant observation that in many instances, protein kinases from parasitic protozoa are phylogenetically distant from those in humans has established this group of enzymes as potential drug targets in the Malaria parasite. One of the differences from the host kinome identified in Plasmodia was the presence of calcium dependent protein kinases (CDPKs), normally only found in plants. In order to rationally design novel inhibitors and chemical tools exclusively targeting CDPKs, reliable molecular structures are needed. High resolution structures will also enable in silico screening to identify new leads. Structural Bioinformatics, specifically molecular modelling, can contribute immensely to improving access to structural information for these challenging targets. Here, a three dimensional structure of PfCDPK4 created by homology modelling is reported. Further, the model is used as a receptor for in silico screening of a large chemical library. Future work will aim to screen a prioritised subset of the library in vitro and to study the structures of PfCDPK4 in complex with identified hits by X-ray crystallography.
Plant molecular pharming to overcome the global impact of neglected tropical diseases
(Springer, 2024-04) Moralo, Maabo; Singh, Advaita A; Pillay, Priyen; Kwezi, Lusisizwe; Tsekoa, Tsepo L
Neglected tropical diseases (NTD) include a broad group of diseases that affect close to two billion people mainly from low and lower-middle income countries. NTD’s account for 12% of the global disease burden and approximately 200,000 deaths annually. The updated 2017 World Health Organisation’s NTD list recognises 20 major NTDs, 19 of these are infectious diseases caused by helminths, protozoa, bacteria or viruses. Snakebite envenoming is the only non-infectious disease on the list, and it has been included due to its high disease burden and impact, especially on young people and children. Global interventions for achieving 90% reduction in NTD treatment by 2030 NTD include prevention, control, elimination and eradication strategies. However, there are still gaps in the research and development of therapeutics and vaccines and limited access to therapeutics, vaccines and diagnostics. This chapter broadly discusses NTDs, progress made and the insufficiencies in the landscape of therapeutics and vaccines and the critical role of plant molecular farming in response to the global disease burden of NTDs. Plant molecular farming presents an opportunity to develop new cost-effective NTD-targeting therapeutics and vaccines and cost-effective NTD diagnostic tools for increased equitable access by vulnerable populations in resource-limited settings.
Plant-based production of highly potent anti-HIV antibodies with engineered posttranslational modifications
(2020-04) Singh, Advaita Acarya; Pooe, O; Kwezi, Lusisizwe; Lotter-Stark, T; Stoychev, Stoyan H; Alexandra, Kabamba B; Gerber, Isak B; Bhiman, JN; Vorster, J; Pauly, M; Zeitlin, L; Whaley, K; Mach, L; Steinkellner, H; Morris, L; Tsekoa, Tsepo L; Chikwamba, Rachel K
Broadly neutralising antibodies (bNAbs) against human immunodeficiency virus type 1 (HIV-1), such as CAP256-VRC26 are being developed for HIV prevention and treatment. These Abs carry a unique but crucial post-translational modification (PTM), namely O-sulfated tyrosine in the heavy chain complementarity determining region (CDR) H3 loop. Several studies have demonstrated that plants are suitable hosts for the generation of highly active anti-HIV-1 antibodies with the potential to engineer PTMs. Here we report the expression and characterisation of CAP256-VRC26 bNAbs with posttranslational modifications (PTM). Two variants, CAP256-VRC26 (08 and 09) were expressed in glycoengineered Nicotiana benthamiana plants. By in planta co-expression of tyrosyl protein sulfotransferase 1, we installed O-sulfated tyrosine in CDR H3 of both bNAbs. These exhibited similar structural folding to the mammalian cell produced bNAbs, but non-sulfated versions showed loss of neutralisation breadth and potency. In contrast, tyrosine sulfated versions displayed equivalent neutralising activity to mammalian produced antibodies retaining exceptional potency against some subtype C viruses. Together, the data demonstrate the enormous potential of plant-based systems for multiple posttranslational engineering and production of fully active bNAbs for application in passive immunisation or as an alternative for current HIV/AIDS antiretroviral therapy regimens.
A plant-biotechnology approach for producing highly potent anti-HIV antibodies for antiretroviral therapy consideration
(2021-12) Singh, Advaita A; Pillay, Priyen; Kwezi, Lusisizwe; Tsekoa, Tsepo L
Despite a reduction in global HIV prevalence the development of a pipeline of new therapeutics or pre-exposure prophylaxis to control the HIV/AIDS epidemic are of high priority. Antibody-based therapies offer several advantages and have been shown to prevent HIV-infection. Plant-based production is efficient for several biologics, including antibodies. We provide a short review on the work by Singh et al., 2020 who demonstrated the transient production of potent CAP256-VRC26 broadly neutralizing antibodies. These antibodies have engineered posttranslational modifications, namely N-glycosylation in the fragment crystallizable region and O-sulfation of tyrosine residues in the complementary-determining region H3 loop. The glycoengineered Nicotiana benthamiana mutant ( XTFT) was used, with glycosylating structures lacking ß1,2-xylose and/or a1,3-fucose residues, which is critical for enhanced effector activity. The CAP256-VRC26 antibody lineage targets the first and second variable region of the HIV-1 gp120 envelope glycoprotein. The high potency of this lineage is mediated by a protruding O-sulfated tyrosine in the CDR H3 loop. Nicotiana benthamiana lacks human tyrosyl protein sulfotransferase 1, the enzyme responsible for tyrosine O-sulfation. The transient coexpression of the CAP256-VRC26 antibodies with tyrosyl protein sulfotransferase 1 in planta had restored the efficacy of these antibodies through the incorporation of the O-sulfation modification. This approach demonstrates the strategic incorporation of posttranslational modifications in production systems, which may have not been previously considered. These plant-produced CAP256-VRC26 antibodies have therapeutic as well as topical and systemic pre-exposure prophylaxis potential in enabling the empowerment of young girls and women given that gender inequalities remain a major driver of the epidemic.
Plant-produced Bluetongue chimaeric VLP vaccine candidates elicit serotype-specific immunity in sheep
(Elsevier BV, 2019-09) Mokoena, NB; Moetlhoa, B; Rutkowska, Daria A; Mamputha, Sipho; Dibakwane, VS; Tsekoa, Tsepo L; O’Kennedy, Martha M
Bluetongue (BT) is a hemorrhagic non-contagious, biting midge-transmitted disease of wild and domestic ruminants that is caused by bluetongue virus (BTV). Annual vaccination plays a pivotal role in BT disease control in endemic regions. Due to safety concerns of the current BTV multivalent live attenuated vaccine (LAV), a safe efficacious new generation subunit vaccine such as a plant-produced BT virus-like particle (VLP) vaccine is imperative. Previously, homogenous BTV serotype 8 (BTV-8) VLPs were successfully produced in Nicotiana benthamiana plants and provided protective immunity in sheep. In this study, combinations of BTV capsid proteins from more than one serotype were expressed and assembled to form chimaeric BTV-3 and BTV-4 VLPs in N. benthamiana plants. The assembled homogenous BTV-8, as well as chimaeric BTV-3 and chimaeric BTV-4 VLP serotypes, were confirmed by SDS-PAGE, Transmission Electron microscopy (TEM) and protein confirmation using liquid chromatography-mass spectrometry (LC-MS/MS) based peptide sequencing. As VP2 is the major determinant eliciting protective immunity, the percentage coverage and number of unique VP2 peptides detected in assembled chimaeric BT VLPs were used as a guide to assemble the most appropriate chimaeric combinations. Both plant-produced chimaeric BTV-3 and BTV-4 VLPs were able to induce long-lasting serotype-specific neutralizing antibodies equivalent to the monovalent LAV controls. Antibody levels remained high to the end of the trial. Combinations of homogenous and chimaeric BT VLPs have great potential as a safe, effective multivalent vaccine with the ability to distinguish between vaccinated and infected individuals (DIVA) due to the absence of non-structural proteins.
Recombinant expression, purification and PEGylation of DNA Ligases
(2022-04) Zuma, LK; Gasa, NL; Mazibuko, X; Simelane, BC; Pillay, Priyen; Kwezi, Lusisizwe; Tsekoa, Tsepo L; Pooe, OJ
Background: Reagent proteins such as DNA ligases play a central role in the global reagents market. DNA ligases are routinely used and are vital in academic and science research environments. Their major functions include sealing nicks by linking the 5'-phosphorylated end to a 3'-hydroxyl end on the phosphodiester backbone of DNA, utilizing ATP or NADP molecules as an energy source. Objective: The current study sought to investigate the role of PEGylation on the biological activity of purified recombinant DNA ligases. Method: We produced two recombinant DNA ligases (Ligsv081 and LigpET30) using E. coli expression system and subsequently purified using affinity chromatography. The produced proteins were conjugated to site specific PEGylation or non-specific PEGylation. FTIR and UV-VIS spectroscopy were used to analyze secondary structures of the PEG conjugated DNA ligases. Differential scanning fluorimetry was employed to assess the protein stability when subjected various PEGylation conditions. Results: In this study, both recombinant DNA ligases were successfully expressed and purified as homogenous proteins. Protein PEGylation enhanced ligation activity, increased transformation efficiency by 2-fold for plasmid ligations and reduced the formation of protein aggregates. Conclusion: Taken together, site-specific PEGylation can potentially be explored to enhance the biological activity and stability of reagent proteins such as ligases.
Safety and immunogenicity of plant-produced African horse sickness virus-like particles in horses
(BioMed Central, 2018-10) Dennis, SJ; O'Kennedy, Maretha M; Rutkowska, Daria A; Tsekoa, Tsepo L; Lourens, Carina W; Hitzeroth, II; Meyers, AE; Rybicki, EP
African horse sickness (AHS) is caused by multiple serotypes of the dsRNA AHSV and is a major scourge of domestic equids in Africa. While there are well established commercial live attenuated vaccines produced in South Africa, risks associated with these have encouraged attempts to develop new and safer recombinant vaccines. Previously, we reported on the immunogenicity of a plant-produced AHS serotype 5 virus-like particle (VLP) vaccine, which stimulated high titres of AHS serotype 5-specific neutralizing antibodies in guinea pigs. Here, we report a similar response to the vaccine in horses. This is the first report demonstrating the safety and immunogenicity of plant-produced AHS VLPs in horses.
The study of degradation mechanisms of glyco-engineered plant produced anti-rabies monoclonal antibodies E559 and 62-71-3
(Public Library of Science, 2018-12) Buthelezi, Sindisiwe G; Dirr, HW; Chakauya, Ereck; Chikwamba, Rachel K; Martens, L; Tsekoa, Tsepo L; Vandermarliere, E; Stoychev, Stoyan H
Rabies is an ancient and neglected zoonotic disease caused by the rabies virus, a neurotropic RNA virus that belongs to the Rhabdoviridae family, genus Lyssavirus. It remains an important public health problem as there are cost and health concerns imposed by the current human post exposure prophylaxis therapy. The use of monoclonal antibodies (mAbs) is therefore an attractive alternative. Rabies mostly affects people that reside in resource-limited areas where there are occasional failures in the cold-chain. These environmental changes may upset the stability of the mAbs. This study focused on mAbs 62-71-3 and E559; their structures, responses to freeze/thaw (F/T) and exposure to reactive oxygen species were therefore studied with the aid of a wide range of biophysical and in silico techniques in order to elucidate their stability and identify aggregation prone regions. E559 was found to be less stable than 62-71-3. The complementarity determining regions (CDR) contributed the most to its instability, more specifically: peptides 99EIWD102 and 92ATSPYT97 found in CDR3, Trp33 found in CDR1 and the oxidised Met34. The constant region “158SWNSGALTGHTFPAVL175” was also flagged by the special aggregation propensity (SAP) tool and F/T experiments to be highly prone to aggregation. The E559 peptides “4LQESGSVL11 from the heavy chain and 4LTQSPSSL11 from the light chain, were also highly affected by F/T. These residues may serve as good candidates for mutation, in the aim to bring forward more stable therapeutic antibodies, thus paving a way to a more safe and efficacious antibody-based cocktail treatment against rabies.
Transient proteolysis reduction of Nicotiana benthamiana-produced CAP256 broadly neutralizing antibodies using CRISPR/Cas9
(2022-08) Singh, Advaita A; Pillay, Priyen; Naicker, Previn; Alexandre, Kabamba B; Malatji, Kanyane; Mach, L; Steinkellner, H; Vorster, J; Chikwamba, Rachel K; Tsekoa, Tsepo L
The hypersensitive response is elicited by Agrobacterium infiltration of Nicotiana benthamiana, including the induction and accumulation of pathogenesis-related proteins, such as proteases. This includes the induction of the expression of several cysteine proteases from the C1 (papain-like cysteine protease) and C13 (legumain-like cysteine protease) families. This study demonstrates the role of cysteine proteases: NbVPE-1a, NbVPE-1b, and NbCysP6 in the proteolytic degradation of Nicotiana benthamiana (glycosylation mutant XTFT)-produced anti-human immunodeficiency virus broadly neutralizing antibody, CAP256-VRC26.25. Three putative cysteine protease cleavage sites were identified in the fragment crystallizable region. We further demonstrate the transient coexpression of CAP256-VRC26.25 with CRISPR/Cas9-mediated genome editing vectors targeting the NbVPE-1a, NbVPE-1b, and NbCysP6 genes which resulted in a decrease in CAP256-VRC26.25 degradation. No differences in structural features were observed between the human embryonic kidney 293 (HEK293)-produced and XTFT broadly neutralizing antibodies produced with and without the coexpression of genome-editing vectors. Furthermore, despite the presence of proteolytically degraded fragments of plant-produced CAP256-VRC26.25 without the coexpression of genome editing vectors, no influence on the in vitro functional activity was detected. Collectively, we demonstrate an innovative in planta strategy for improving the quality of the CAP256 antibodies through the transient expression of the CRISPR/Cas9 vectors.

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