RU2491293C2 - Иммунологические анализы активности ботулинического токсина серотипа а - Google Patents

Иммунологические анализы активности ботулинического токсина серотипа а Download PDF

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RU2491293C2
RU2491293C2 RU2010140478/10A RU2010140478A RU2491293C2 RU 2491293 C2 RU2491293 C2 RU 2491293C2 RU 2010140478/10 A RU2010140478/10 A RU 2010140478/10A RU 2010140478 A RU2010140478 A RU 2010140478A RU 2491293 C2 RU2491293 C2 RU 2491293C2
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bont
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antibody
epitope
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Эстер ФЕРНАНДЕЗ-САЛАС
Джоанн ВАНГ
Паттон Е. ГЭРЭЙ
Лина С. ВОНГ
Д. Дайанн ХОДЖЕС
Кей Роджер АОКИ
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Аллерган, Инк.
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Abstract

В изобретении раскрыта композиция для продукции антител SNAP-25, способных связываться с эпитопом, содержащим C-конец (карбоксильный) на остатке P1 расщепляемой связи сайта расщепления BoNT/A продукта расщепления SNAP-25, содержащая носитель, гибкий линкер, содержащий по меньшей мере три аминокислоты, и антиген SNAP-25, для которого приведена аминокислотная последовательность. Описаны варианты антител α-SNAP-25 с указанной выше способностью и их использование в способе обнаружения активности BoNT/A с использованием клеток из стабильной клеточной линии, чувствительных к интоксикации BoNT/A, и способе определения иммунорезистентности к BoNT/A у млекопитающего с использованием тестируемого образца от животного и клеток стабильной клеточной линии, клетки которой чувствительны к интоксикации BoNT/A. Использование изобретения обеспечивает надежность, простоту и позволяет исключить из анализов ботулинического токсина необходимость тестирования на животных. 7 н. и 8 з.п. ф-лы, 11 ил., 14 табл., 12 пр.

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Claims (15)

1. Композиция для продукции антител α-SNAP-25, которые могут связываться с эпитопом, содержащим С-конец (карбоксильный) на остатке P1 расщепляемой связи сайта расщепления BoNT/A продукта расщепления SNAP-25, содержащая носитель, гибкий линкер и антиген SNAP-25, где гибкий линкер содержит по меньшей мере три аминокислоты, и антиген SNAP-25 содержит аминокислотную последовательность, приведенную на SEQ ID NO:148.
2. Композиция по п.2, где аминокислотная последовательность гибкого линкера и антигена SNAP-25 представляет собой аминокислотную последовательность, приведенную на SEQ ID NO:38.
3. Выделенное антитело α-SNAP-25,
где выделенное антитело α-SNAP-25 связывается с эпитопом, содержащим C-концевой глутамин расщепляемой связи сайта расщепления BoNT/A продукта расщепления SNAP-25;
где антитело a-SNAP-25 имеет константу скорости ассоциации для эпитопа, не содержащего C-концевой глутамин расщепляемой связи сайта расщепления BoNT/A продукта расщепления SNAP-25, составляющую менее 1·101 M-1 с1; и где антитело α-SNAP-25 имеет равновесную константу диссоциации для эпитопа, составляющую менее 0,450 нМ.
4. Выделенное антитело α-SNAP-25 по п.3, где эпитоп представляет собой аминокислотную последовательность, приведенную на SEQ ID NO:32.
5. Выделенное антитело α-SNAP-25, связывающееся с эпитопом, содержащим C-концевой глутамин расщепляемой связи сайта расщепления BoNT/A продукта расщепления SNAP-25, содержащее:
а. вариабельную область тяжелой цепи, содержащую аминокислотную последовательность, приведенную на SEQ ID NO:72, SEQ ID NO:74, SEQ ID NO:76, SEQ ID NO:80 или SEQ ID NO:82; и
б. вариабельную область легкой цепи, содержащую аминокислотную последовательность, приведенную на SEQ ID NO:84, SEQ ID NO:86, SEQ ID NO:88, SEQ ID NO:90 или SEQ ID NO:92.
6. Выделенное антитело α-SNAP-25, связывающееся с эпитопом, содержащим C-концевой глутамин расщепляемой связи сайта расщепления BoNT/A продукта расщепления SNAP-25, содержащее:
а. вариабельную область тяжелой цепи, содержащую аминокислотную последовательность, приведенную на SEQ ID NO:93, SEQ ID NO:121 или SEQ ID NO:100; и
б. вариабельную область легкой цепи, содержащую аминокислотную последовательность, приведенную на SEQ ID NO:105, SEQ ID NO:110 или SEQ ID NO:115.
7. Выделенное антитело α-SNAP-25, связывающееся с эпитопом, содержащим C-концевой глутамин расщепляемой связи сайта расщепления BoNT/A продукта расщепления SNAP-25, содержащее по меньшей мере VH CDR3, имеющий аминокислотную последовательность, приведенную на SEQ ID NO:100, VH CDR3, имеющий аминокислотную последовательность, приведенную на SEQ ID NO:101 или VH CDR3, имеющий аминокислотную последовательность, приведенную на SEQ ID NO:102.
8. Способ обнаружения активности BoNT/A, включающий стадии:
а. обработки клетки из стабильной клеточной линии образцом, содержащим BoNT/A, где клетка из стабильной клеточной линии чувствительна к интоксикации BoNT/A в концентрации BoNT/A приблизительно 500 пМ или менее;
б. выделения из обработанной клетки компонента SNAP-25, содержащего продукт расщепления SNAP-25, имеющий С-концевой глутамин расщепляемой связи сайта расщепления BoNT/A;
в. приведения в контакт компонента SNAP-25 с антителом α-SNAP-25, связанным с твердофазным носителем,
где антитело α-SNAP-25 связывается с эпитопом, содержащим C-концевой глутамин расщепляемой связи сайта расщепления BoNT/A продукта расщепления SNAP-25, где антитело α-SNAP-25 имеет константу скорости ассоциации для эпитопа из SNAP-25, не содержащего C-концевой глутамин расщепляемой связи сайта расщепления BoNT/A продукта расщепления SNAP-25, составляющую менее 1·101 M-1 c-1; и антитело α-SNAP-25 имеет равновесную константу диссоциации для эпитопа, составляющую мене 0,450 нМ;
г.обнаружения наличия комплекса антиген-антитело, содержащего антитело α-SNAP-25 и продукт расщепления SNAP-25, имеющий C-концевой глутамин расщепляемой связи сайта расщепления BoNT/A;
где обнаружение при помощи комплекса антиген-антитело является показателем активности BoNT/A.
9. Способ по п.8, где продукт расщепления SNAP-25 представляет собой SNAP-25197.
10. Способ по п.8, где присутствие комплекса антиген-антитело обнаруживают с использованием сэндвич ИФА.
11. Способ по п.8, где способ имеет отношение сигнала к шуму на нижней асимптоте по меньшей мере 3:1 и отношение сигнала к шуму на верхней асимптоте по меньшей мере 10:1.
12. Способ по п.8, где образец содержит максимально 100 пМ BoNT/A.
13. Способ по п.8, где клетка из стабильной клеточной линии чувствительна к интоксикации BoNT/A в концентрации BoNT/A приблизительно 100 пМ или менее.
14. Способ по п.8, где способ осуществляют в моноплексном варианте или мультиплексном варианте.
15. Способ определения иммунорезистентности к BoNT/A у млекопитающего, включающий стадии:
а. добавления BoNT/A к тестируемому образцу, полученному у млекопитающего, тестируемого на наличие или отсутствие антител, нейтрализующих α-BoNT/A;
б. обработки клетки из стабильной клеточной линии тестируемым образцом, где клетка из стабильной клеточной линии чувствительна к интоксикации BoNT/A;
в. выделения из обработанных клеток компонента SNAP-25, содержащего продукт расщепления SNAP-25, имеющего C-концевой глутамин расщепляемой связи сайта расщепления BoNT/A;
г. приведения в контакт компонента SNAP-25 с антителом α-SNAP-25, связанным с твердофазным носителем;
где антитело α-SNAP-25 связывается с эпитопом, содержащим C-концевой глутамин расщепляемой связи сайта расщепления BoNT/A продукта расщепления SNAP-25, где антитело α-SNAP-25 имеет константу скорости ассоциации для эпитопа из SNAP-25, не содержащего С-концевой глутамин расщепляемой связи сайта расщепления BoNT/A продукта расщепления SNAP-25, составляющую менее 1·101 M-1 с-1; и антитело α-SNAP-25 имеет равновесную константу диссоциации для эпитопа, составляющую менее 0,450 нМ;
д. обнаружения наличия комплекса антиген-антитело, содержащего антитело α-SNAP-25 и продукт расщепления SNAP-25, имеющий C-концевой глутамин расщепляемой связи сайта расщепления BoNT/A;
е. повторения стадий б-д с отрицательным контрольным образцом вместо тестируемого образца, где отрицательный контрольный образец содержит BoNT/A и сыворотку, о которой известно, что она не содержит нейтрализующие антитела α-BoNT/A; и
ж. сравнения количества комплекса антиген-антитело, обнаруженного на стадии д, с количеством комплекса антиген-антитело, обнаруженного на стадии е,
где обнаружение меньшего количества комплекса антиген-антитело, обнаруженного на стадии д, по сравнению с количеством комплекса антиген-антитело, обнаруженного на стадии е, является показателем присутствия нейтрализующих антител α-BoNT/A.
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