Cloning and sequencing of a complete myosin heavy chain cDNA from Schistosoma mansoni

Weston, David S.; Schmitz, Jutta; Kemp, Walter M.; Kunz, Werner

doi:10.1016/0166-6851(93)90100-c

Cited by 15 publications

(7 citation statements)

References 14 publications

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“…Proposed additional smaller isoforms in the experimental study [29] are most probably artefacts from proteolysis. The transcript sequence determined from a muscle myosin from adult Schistosoma mansoni [31] is identical to the sequence derived from genomic DNA as reported here. Mutually exclusive exon A (5′ exon of the cluster) is included in this sequence implying that exon B is the version spliced into the larval Mhc transcript.…”

Section: Resultssupporting

confidence: 62%

Shared Gene Structures and Clusters of Mutually Exclusive Spliced Exons within the Metazoan Muscle Myosin Heavy Chain Genes

Kollmar

Hatje

2014

PLoS ONE

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Multicellular animals possess two to three different types of muscle tissues. Striated muscles have considerable ultrastructural similarity and contain a core set of proteins including the muscle myosin heavy chain (Mhc) protein. The ATPase activity of this myosin motor protein largely dictates muscle performance at the molecular level. Two different solutions to adjusting myosin properties to different muscle subtypes have been identified so far: Vertebrates and nematodes contain many independent differentially expressed Mhc genes while arthropods have single Mhc genes with clusters of mutually exclusive spliced exons (MXEs). The availability of hundreds of metazoan genomes now allowed us to study whether the ancient bilateria already contained MXEs, how MXE complexity subsequently evolved, and whether additional scenarios to control contractile properties in different muscles could be proposed, By reconstructing the Mhc genes from 116 metazoans we showed that all intron positions within the motor domain coding regions are conserved in all bilateria analysed. The last common ancestor of the bilateria already contained a cluster of MXEs coding for part of the loop-2 actin-binding sequence. Subsequently the protostomes and later the arthropods gained many further clusters while MXEs got completely lost independently in several branches (vertebrates and nematodes) and species (for example the annelid Helobdella robusta and the salmon louse Lepeophtheirus salmonis). Several bilateria have been found to encode multiple Mhc genes that might all or in part contain clusters of MXEs. Notable examples are a cluster of six tandemly arrayed Mhc genes, of which two contain MXEs, in the owl limpet Lottia gigantea and four Mhc genes with three encoding MXEs in the predatory mite Metaseiulus occidentalis. Our analysis showed that similar solutions to provide different myosin isoforms (multiple genes or clusters of MXEs or both) have independently been developed several times within bilaterian evolution.

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Section: Resultssupporting

confidence: 62%

Shared Gene Structures and Clusters of Mutually Exclusive Spliced Exons within the Metazoan Muscle Myosin Heavy Chain Genes

Kollmar

Hatje

2014

PLoS ONE

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“…The complete cDNA sequence of the myosin heavy chain of S. mansoni is known (30). Our sequence analyses of the phage clone suggest that the myosin that bound to PZQ is regulatory MLC.…”

Section: Discussionmentioning

confidence: 87%

Praziquantel Affects the Regulatory Myosin Light Chain of Schistosoma mansoni

Munirathinam

Salunkhe

Mallia

et al. 2009

Antimicrob Agents Chemother

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Praziquantel (PZQ) is the drug of choice for schistosomiasis and probably is the only highly effective drug currently available for treating schistosomiasis-infected individuals. The mode of action of PZQ involves increasing the calcium uptake of the parasite, resulting in tegumental damage and death of the parasite. Despite its remarkable function, the target of PZQ has not been identified yet. To begin to understand where PZQ acts, in this study we expressed the cDNA library of Schistosoma mansoni on the surface of T7 bacteriophages and screened this library with labeled PZQ. This procedure identified a clone that strongly bound to PZQ. Subsequent DNA analysis of inserts showed that the clone coded for regulatory myosin light chain protein. The gene was then cloned, and recombinant S. mansoni myosin light chain (SmMLC) was expressed. Immunoblot analysis using antibodies raised to recombinant SmMLC (rSmMLC) showed that SmMLC is abundantly expressed in schistosomula and adult stages compared to the amount in cercarial stages. In vitro analyses also confirmed that PZQ strongly binds to rSmMLC. Further, peptide mapping studies showed that PZQ binds to amino acids 46 to 76 of SmMLC. Immunoprecipitation analysis confirmed that SmMLC is phosphorylated in vivo upon exposure to PZQ. Interestingly, significant levels of anti-SmMLC antibodies were present in vaccinated mice compared to the amount in infected mice, suggesting that SmMLC may be a potential target for protective immunity in schistosomiasis. These findings suggest that PZQ affects SmMLC function, and this may have a role in PZQ action.

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“…Average distance tree for MHC II sequence alignment showing that MHC II is either striated-or smooth-like (cyan or tan, respectively). The schistosome MHC II (Q02456), highlighted in yellow was demonstrated to be present at the transcription level (80) and in the thick filament homogenate by proteomic analysis (Fig. 3); it was compared with complete sequences of the other myosins shown.…”

Section: Resultsmentioning

confidence: 99%

An invertebrate smooth muscle with striated muscle myosin filaments

Sulbarán

Álamo

Pinto

et al. 2015

Proc. Natl. Acad. Sci. U.S.A.

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Muscle tissues are classically divided into two major types, depending on the presence or absence of striations. In striated muscles, the actin filaments are anchored at Z-lines and the myosin and actin filaments are in register, whereas in smooth muscles, the actin filaments are attached to dense bodies and the myosin and actin filaments are out of register. The structure of the filaments in smooth muscles is also different from that in striated muscles. Here we have studied the structure of myosin filaments from the smooth muscles of the human parasite Schistosoma mansoni. We find, surprisingly, that they are indistinguishable from those in an arthropod striated muscle. This structural similarity is supported by sequence comparison between the schistosome myosin II heavy chain and known striated muscle myosins. In contrast, the actin filaments of schistosomes are similar to those of smooth muscles, lacking troponin-dependent regulation. We conclude that schistosome muscles are hybrids, containing striated muscle-like myosin filaments and smooth muscle-like actin filaments in a smooth muscle architecture. This surprising finding has broad significance for understanding how muscles are built and how they evolved, and challenges the paradigm that smooth and striated muscles always have distinctly different components.thick filament | muscle structure | muscle contraction | schistosome | Schistosoma mansoni

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Cloning and sequencing of a complete myosin heavy chain cDNA from Schistosoma mansoni

Cited by 15 publications

References 14 publications

Shared Gene Structures and Clusters of Mutually Exclusive Spliced Exons within the Metazoan Muscle Myosin Heavy Chain Genes

Shared Gene Structures and Clusters of Mutually Exclusive Spliced Exons within the Metazoan Muscle Myosin Heavy Chain Genes

Praziquantel Affects the Regulatory Myosin Light Chain of Schistosoma mansoni

An invertebrate smooth muscle with striated muscle myosin filaments

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