The Present Status of Tetanus and Tetanus Vaccination

Gałazka, A; Gasse, François

doi:10.1007/978-3-642-85173-5_2

Cited by 46 publications

(47 citation statements)

References 45 publications

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“…In fact, this disease is completely prevented by immunization with tetanus toxoid, i.e., formaldehyde-treated TeNT (3). TeNT is produced by Clostridium tetani as a single polypeptide chain of 150 kDa and is activated by proteolytic cleavage with formation of a 50-kDa chain (L) and a 100-kDa chain (H) linked by a single interchain disulfide bridge and by noncovalent forces (4).…”

Section: Tetanus Toxin (Tent)mentioning

confidence: 99%

Recombinant and Truncated Tetanus Neurotoxin Light Chain: Cloning, Expression, Purification, and Proteolytic Activity

Tonello

Pellizzari

Pasqualato

et al. 1999

Protein Expression and Purification

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Section: Tetanus Toxin (Tent)mentioning

confidence: 99%

Recombinant and Truncated Tetanus Neurotoxin Light Chain: Cloning, Expression, Purification, and Proteolytic Activity

Tonello

Pellizzari

Pasqualato

et al. 1999

Protein Expression and Purification

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“…Tetanoz olgular›n›n y›llara göre da¤›l›m› incelendi¤inde tüm ülkelerde son on y›l içerisinde y›ll›k görül-me s›kl›¤›n›n yaklafl›k yar›s› kadar azald›¤› görülmektedir. Ancak, gerçek s›kl›k ço¤unlukla bildirilenden daha fazlad›r (5,6).…”

Section: Tart›flmaunclassified

A five-year-old boy with fever, headache, disturbances in walking, erect posture and speech - Case of the Month

Arıca¹,

Arıca²,

Gücük³

et al. 2010

tpa

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, , b ba afl fl a a¤ ¤r r› ›s s› ›, , y yü ür rü üm me e, , d di ik k d du ur rm ma a v ve e k ko on nu ufl flm ma ad da a b bo oz zu uk kl lu uk kl la a b ba afl flv vu ur ra an n b be efl fl y ya afl fl› ›n nd da a e er rk ke ek k h ha as st ta a A A f fi iv ve e--y ye ea ar r--o ol ld d b bo oy y w wi it th h f fe ev ve er r, , h he ea ad da ac ch he e, , d di is st tu ur rb ba an nc ce es s i in n w wa al lk ki in ng g, , e er re ec ct t p po os st tu ur re e a an nd d s sp pe ee ec ch h M Me es su ut t O Ok ku ur r, , A Av vn ni i K Ka ay ya a, , L Lo ok km ma an n Ü Üs st ty yo ol l, , E Er rt ta an n S Sa al l, , H Hü üs se ey yi in n Ç Ça ak ks se en n A Ay y› ›n n O Ol lg gu us su u C Ca as se e o of f t th he e M Mo on nt th h 3 30 03 3 Olgu sunumuBefl yafl›nda erkek hasta, bir hafta önce bafllayan atefl, bafl a¤r›s›, huzursuzluk, yürümede bozulma, dik duramama ve konuflurken difllerini s›kma yak›nmalar›yla getirildi. Hikayesinden on gün önce koflarken yere düfl-tü¤ü, sol dirsek ve dizinin yaraland›¤›, ancak bunun için herhangi bir sa¤l›k kurulufluna baflvurmad›¤› ö¤renildi.Öz geçmiflinden afl›lar›n›n düzenli olarak yap›lmad›¤› saptand›. Bunun d›fl›nda özellik yoktu.Soy Tan› TetanozMevcut bulgularla tetanoz düflünülen hasta çocuk yo¤un bak›m birimine yat›r›larak damardan 300 000 Ü/kg/gün 6 dozda kristalize penisilin ve iki saatte bir rektal diyazepam tedavisi baflland›. Tetanoz immünglobuli-ni (T‹G) 100 Ü/kg dozunda kas içi yoldan uyguland›. Yat›fl›n›n üçüncü günü rektal diyazepam uygulamas› sonland›r›larak a¤›zdan diyazepam uygulamas›na geçildi. Hastan›n yat›fl›n yedinci günü aya¤a kalkabildi¤i dokuzuncu günü ise yürümeye bafllad›¤› görüldü. Yat›fl›n›n 11. günü antibiyotik tedavisi tamamlanan hasta diyazepam tedavisine devam edilerek yat›fl›n›n 14. günü flifa ile taburcu edildi. Bir hafta sonraki poliklinik kontrolünde hastan›n diyazepam tedavisi de sonland›r›ld›. Hastada tetanoza ba¤l› her hangi bir komplikasyon geliflmedi. Tart›flmaTetanoz; C. tetani'nin salg›lad›¤› toksinle oluflan, kaslarda yayg›n tonus art›fl›, aral›kl› kas spazmlar› ve sempatik aktivite art›fl› ile giden ölüm yüzdesi çok yüksek bir hastal›kt›r. Tetanospazmin isimli nörotoksin ile inhibitör nöronlarda nörotransmiter sal›n›m›n› bozarak periferik kaslarda sertlik ve spazmlara yol açar (1).Yaralanma sonras› geliflen tetanoz tutulan kaslar›n yerleflimine göre yayg›n, yerel ve sefalik tipte olabilir. Olgular›n ço¤u yayg›n tiptedir, di¤er tipler daha nadir görülür (1).Trismus ve opistotonus yayg›n tetanozun bilinen klinik özelliklerindendir (2). Ne var ki, yayg›n tetanoz enfeksiyonu her zaman bu belirti ve bulgularla kendini göstermez. Ör-ne¤in sadece orofaringeal belirtiler ile gelebilir ve daha s›k-l›kla peritonsiller apse gibi orofaringeal enfeksiyon olarak yanl›fl tan› konulabilir. Ancak, tan›nmayan tetanoz fliddetli kas spazmlar›, otonomik disfonksiyon ve/veya solunum yetersizli¤i ile h›zla kritik bir durum içine ilerleyebilir (3).Toplumdaki bireylerin tümü yaflamlar›n›n herhangi bir döneminde tetanoz etkeni ile karfl›laflma risk...

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“…The basic mode of action is similar in all CNTs; they cleave a specific family of proteins integral to the exocytotic process (i.e. soluble NSF attachment protein receptor), thereby avoiding the synaptic SNARE complex formation that finally ends up in blocking vesicular mediator release to the extra-cellular environment (Chen et al, 2009;Galazka & Gasse, 1995).…”

Section: Introductionmentioning

confidence: 99%

“…The LC is a zinc metalloprotease and contains the catalytic domain of the neurotoxin. This zinc-endo-protease specifically cleaves the neuronal SNARE protein VAMP2 (vesicle associated membrane protein-2) and holds back the release of inhibitory neurotransmitter glycine and g-aminobutyric acid that ultimately leads to spastic paralysis, tetanus (Chen et al, 2009;Galazka & Gasse, 1995). The TeNT HC is composed of two domains, each of approximately 50 kDa; the N-terminal fragment is critical for LC translocation and the C-terminal fragment (Fragment C) is the receptor binding domain (Lalli et al, 1999).…”

Section: Introductionmentioning

confidence: 99%

Characterization of neutralizing monoclonal antibodies directed against tetanus toxin fragment C

Yousefi

Tahmasebi²,

Younesi

et al. 2013

Journal of Immunotoxicology

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Clostridium tetani causes a life-threatening infectious disease by production of tetanus neurotoxin (TeNT), a 150 kDa molecule composed of light (LC) and heavy chain (HC) polypeptides. The TeNT HC contains an N-terminal domain critical for LC translocation and a Cterminal toxin receptor-binding domain known as fragment C. Despite extensive investigations on epitope specificity of anti-TeNT antibodies, the immunodominant neutralizing epitopes of the toxin are poorly defined. This study describes the generation and characterization of four monoclonal antibodies (MAb) specific for TeNT. The characteristics of each MAb were explored in terms of isotype, specificity, affinity, and immuno-globulin heavy chain variable region (IGHV) gene usage using ELISA, Western blotting, and sequencing techniques. The toxin neutralizing activity of the MAbs was also investigated using the in vitro GT1b neutralizing assay. The data demonstrated that all MAbs bind to tetanus toxin and toxoid. Sub-fragments binding analysis showed that two MAbs react with fragment C, one with both fragment C and LC, and one with LC. Only the two fragment C-specific MAbs were able to neutralize the toxin. Sequencing of the expressed VH and VL genes revealed rearrangements of various VH and VL gene segments in all hybridoma clones. Clonality of the hybridomas was also confirmed by a competition assay that showed recognition of distinct epitopes by these MAbs. The results suggest the importance of TeNT fragment C in terms of immunogenicity and toxin neutralization activity.

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The Present Status of Tetanus and Tetanus Vaccination

Cited by 46 publications

References 45 publications

Recombinant and Truncated Tetanus Neurotoxin Light Chain: Cloning, Expression, Purification, and Proteolytic Activity

Recombinant and Truncated Tetanus Neurotoxin Light Chain: Cloning, Expression, Purification, and Proteolytic Activity

A five-year-old boy with fever, headache, disturbances in walking, erect posture and speech - Case of the Month

Characterization of neutralizing monoclonal antibodies directed against tetanus toxin fragment C

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